text:
So yesterday evening my bf and I went to the movies (btw go see Xmen: Days of Future Past if you haven't already, so good!) Antyhoo, to waste some time we stopped in the BBW store just to see what it had this go-round and I immediately got mesmerized by all of the half off ol school wf bulbs. I greedily bought several that I really didn't need and afterwards I felt a bit guilty. So today I decided to go to the BBW in The City to return them.
So I was just moseyin around and surveyin the stock when unexpectedly I saw this....
The store had all of the Summer Sip candles (as y'all already know Pomegranate Spritzer, Clementine Crush and Pineapple Lychee Smoothie didn't make the cut). No wf bulbs though (although the outlet BBW store that I went to the night before had them hidden from view). It also had the same fall White Barn Candles that mysteriously appeared online today - Leaves, Cranberry Woods, Fresh Balsam, Bergamot Woods and Sandalwood Citrus. The store also had Spring Balsam from the Destination Line (which I dunno if it's a repackage of Fresh Balsam or Forest Trail from Lakeside last year) as well as the 3 of the 4 floral Fresh Picked candles - Farmstand Freesia, Majestic Rose, Golden Sunflower. However, the coolest part is the store had the fall Fresh Market candles! I for one was not expectin to see any of these soon so I was quite excited to smell em. Let's just say the excitement wore off very quickly.
I hate to be a Negative Nancy but I just wasn't impressed!
So first, let's talk about the old candles they brought back
Lemon Mint Leaf
Why?! Why does BBW keep pushin this damned scent so hard?! We've seen LML in rotation for 3 years, twice in the fall. Attention BBW - LML is not a fall scent..I repeat..LML IS NOOOOOOT A FAAALLLLL SCEEEENNNNNNT!!! Keep this crap in the spring please and thanks! Don't get me wrong, it's a nice scent..I personally think it smells like a toothpaste/dentist office but it's not offensive or stank by any means. However, it's very inappropriate for fall!
Eucalyptus Mint
Again, why?! Why is this back?! While it's slightly more appropriate than LML, I feel this was an unnecessary choice. BBW could've brought back anything instead of this mess - Spice, Blackberry Spice, Woodland Berries, Pear/Heirloom Pear. Or better yet, something NEW!!! So many fruity fall harvest notes to play with- cranberry, plum, figs, nuts, corn/maize...the possibilities are endless!!! This was an unadulterated lazy ass choice and it kinda pisses me off!
Farmstand Apple
Y'know, I want to like ol FA but I just can't make myself do it. First off, it doesn't smell like an apple fresh out the orchard like the notes suggest; it just smells so artificial and home frangrancey. And that damn oak note just makes it smell so off and strange. I feel like the apple note in say, oh I dunno, Apple Crumble or Spiced Cider or even Cider Lane smells more authentic than this. What BBW needs to do is retire this mess and bring back Autumn Apple instead.
And now for the new stuff...
Harvest Peach
*Juices peaches are at the heart of this sweet blend of cinnamon and autumn spices
At first I didn't know what to think of this one. Part of me was a little optimistic and was hoping this would smell warm and sweet and ooey goeey like a hot peach cobbler; Pumpkin Carving or Blackberry Spice but with peach. However, I had a nagging feeling it was gonna wind up smelling like Market Peach with cinnamon...and that's exactly what it smells like. It's a mix of Market Peach and a hint of Springtime in Provence with the same burnt cinnamon/burnt pumpkin note from Sweet Cinnamon Pumpkin. It's so friggin disgustin and it pisses me off cuz this was such a wasted opportunity. This had the potential of being a fall hit and people would love it just for the newness factor but again BBW decided to be lazy and just threw crap together.
Autumn Mums
*A floral blend of soft mum petals, amber and a hint of sandalwood
When I first heard about this I kinda thought for sure this would be a candle version of a soap that came out last year called New England Autumn Bouquet. I'm about 85-90% sure that that's what it is. It also kinda smells like Provence Garden from the Provence collection. Like the soap, it definitely has an old lady perfume vibe to it. Like Provence Garden, there's an odd fruity like sweetness, thanks to the pear blossom note which again goes back to the Autumn Bouquet theory as apple was in the notes and in BBW world apples notes and pear notes are interchangeable. Anyhoo this candle is nice but far from exciting. I feel like this should have been a body fragrance instead of a candle as it does really smell like a fall inspired perfume or body spray for women.
Heirloom Pumpkin
*The perfect autumn pumpkin, celebrated in an invitingly warm blend of fresh pumpkin, creamy nutmeg and rich brown sugar
And now the star of this collection...and I'm using that term loosely. This was the only one that I liked and that says a lot cuz by and large, I'm not a big fan of pumpkin scents. And frankly, the only reason I like this one is because it smells familiar. Yep, you guessed it...this basically smells like Pumpkin Carving! I'm not sure if it's a repackage or a repackage with a twist; there is a very slight difference. I wanna say this smells slightly sweeter than Pumpkin Carving and doesn't have quite of the same earthiness. And it's a bit more nutmeg-ier.. I dunno, I wish there was a Pumpkin Carving in the store for me to compare. At any rate, there's no denyin that the two smell very VERY similar.I have two theories - this is either a repackage with a twist of Pumpkin Carving or it's a repackage of the elusive and mysterious Pumpkin Woods candles from last year...which basically has the same notes as both PC and HP.
So ummm yeah, not impressed! It's really disappointing cuz I like the look of these - they're super cute and antiquey and down homey. It's really a shame that the scents are boring and uninspired. I'm really hoping that this is just a preview of sorts and that we'll see more BETTER scents in this collection in the coming months. If this is any indication of what this upcoming fall season is going be like at BBW, than I have a bad feeling it's gonna majorly suck! Then again, it's too early to tell. With that said, keep the faith!


text:
Mumbai, March 28 -- Politics is in the air, and Youngistaan is one film that shows the Prime Minister of the country in a different light. Indian cinema is coming of age, and perhaps for the first time ever, the PM of India will be shown to be in a live-in relationship.
Actor Jackky Bhagnani, who plays the lead role, will be seen opposite Neha Sharma in the film that releases today (March 28). "We are showing a modern and progressive PM in the film. We talk about moving ahead with the times and that's what my character Abhimanyu does. Nowadays, living in isn't taboo, and he feels that if he's living with someone, it doesn't mean that he has to get married to the person. He believes that he should get married when the time is right for him, and not get bogged down by expectations. If he's doing his job well, then why should anyone have a problem?" says Jackky.
The film reflects on changing times, but Jackky says the story is unique and presented in an entertaining way. The actor believes that the film will send out a message to society and create awareness. "The film isn't about a live-in relationship per se; it's about getting rid of double standards. Don't be a hypocrite. If you make a mistake, admit it, correct it and move on. If you aren't ready for marriage, it's okay. As long as you are committed to the person, you don't need a piece of paper," says Jackky.

subset: commoncrawl


text:
1. Introduction
Ion-exchange chromatography (IEC) is part of ion chromatography which is an important analytical technique for the separation and determination of ionic compounds, together with ion-partition/interaction and ion-exclusion chromatography [1]. Ion chromatography separation is based on ionic (or electrostatic) interactions between ionic and polar analytes, ions present in the eluent and ionic functional groups fixed to the chromatographic support. Two distinct mechanisms as follows; ion exchange due to competitive ionic binding (attraction) and ion exclusion due to repulsion between similarly charged analyte ions and the ions fixed on the chromatographic support, play a role in the separation in ion chromatography. Ion exchange has been the predominant form of ion chromatography to date [2]. This chromatography is one of the most important adsorption techniques used in the separation of peptides, proteins, nucleic acids and related biopolymers which are charged molecules in different molecular sizes and molecular nature [3-6]. The separation is based on the formation of ionic bonds between the charged groups of biomolecules and an ion-exchange gel/support carrying the opposite charge [7]. Biomolecules display different degrees of interaction with charged chromatography media due to their varying charge properties [8].
The earliest report of ion-exchange chromatography date back to 1850, Thompson studied the adsorption of ammonium ions to soils [9-11]. Spedding and Powell published a series of papers describing practical methods for preparative separation of the rare earths by displacement ion-exchange chromatography in 1947. Beginning in the 1950s, Kraus and Nelson reported numerous analytical methods which are used for metal ions based on separation of their chloride, fluoride, nitrate or sulfate complexes by anion chromatography [12]. In order to separate proteins an ion exchange chromatographic method was reported by Peterson and Sober in 1956. In modern form ion exchange chromatography was introduced by Small, Stevens and Bauman in 1975 [3]. Gjerde et al. published a method for anion chromatography in 1979 and this was followed by a similar method for cation chromatography in 1980 [12]. Ion-exchange chromatography has been used for many years to separate various ionic compounds; cations and anions and still continues to be used. The popularity of ion exchange chromatography has been increased in recent years because this technique allows analysis of wide range of molecules in pharmaceutical, biotechnology, environmental, agricultural and other industries [2].
1.1. Ion exchange mechanism
Ion-exchange chromatography which is designed specifically for the separation of differently charged or ionizable compounds comprises from mobile and stationary phases similar to other forms of column based liquid chromatography techniques [9-11]. Mobil phases consist an aqueous buffer system into which the mixture to be resolved. The stationary phase usually made from inert organic matrix chemically derivative with ionizable functional groups (fixed ions) which carry displaceable oppositely charged ion [11]. Ions which exist in a state of equilibrium between the mobile phase and stationary phases giving rise to two possible formats, anion and cation exchange are referred to as counter ion (Figure 1) [1,13]. Exchangeable matrix counter ions may include protons (H+), hydroxide groups (OH-), single charged mono atomic ions (Na+, K+, Cl-), double charged mono atomic ions (Ca2+, Mg2+), and polyatomic inorganic ions (SO42-, PO43-) as well as organic bases (NR2H+) and acids (COO-) [11]. Cations are separated on cation-exchange resin column and anions on an anion exchange resin column [10]. Separation based on the binding of analytes to positively or negatively charged groups which are fixed on a stationary phase and which are in equilibrium with free counter ions in the mobile phase according to differences in their net surface charge (Figure 1) [13-14].
Ion exchange chromatography involves separation of ionic and polar analytes using chromatographic supports derivatized with ionic functional groups that have charges opposite that of the analyte ions. The analyte ions and similarly charged ions of the eluent compete to bind to the oppositely charged ionic functional group on the surface of the stationary phase. Assuming that the exchanging ions (analytes and ions in the mobile phase) are cations, the competition can be explained using the following equation;
In this process the cation M+ of the eluent replaced with the analyte cation C+ bound to the anion X- which is fixed on the surface of the chromatographic support (S).
In anion exchange chromatography, the exchanging ions are anions and the equation is represented as follow;
The anion B- of the eluent replaced with the analyte cation A- bound to the positively charged ion X+ on the surface of the stationary phase. The adsorption of the analyte to the stationary phase and desorption by the eluent ions is repeated during their journey in the column, resulting in the separation due to ion-exchange [2].
Molecules vary considerably in their charge properties and will exhibit different degrees of interaction with charged chromatography support according to differences in their overall charge, charge density and surface charge distribution. Net surface charge of all molecules with ionizable groups is highly pH dependent [13]. Therefore pH of the mobile phase should be selected according to the net charge on a protein of interest within a mixture is opposite to that of matrix functional group, that it will displace the functional group counter ion and bind the matrix. On the other hand oppositely charged proteins will not be retained. Adsorbed protein analytes can be eluted by changing the mobile phase pH which effect the net charge of adsorbed protein, so its matrix binding capacity. Moreover increasing the concentration of a similarly charged species within the mobile phase can be resulted in elution of bound proteins. During ion exchange chromatography for example in anion exchange as illustrated in Figure 2, negatively charged protein analytes can be competitively displaced by the addition of negatively charged ions. The affinity of interaction between the salt ions and the functional groups will eventually exceed that the interaction exists between the protein charges and the functional groups, resulting in protein displacement and elution by increasing gradually the salt concentration in the mobile phase [11].
Complex mixtures of anions or cations can usually be separated and quantitative amounts of each ion measured in a relatively short time by ion exchange chromatography [10]. In classical ion-exchange chromatography separations have been performed in the open-column mode. Column which is loosely packed with stationary phase as small particles made of 1-2 cm diameter glass. The mobile phase or eluent contains the competing ion and is passed continuously into the column and percolates through it under gravity. Sample mixture is applied to the top of the column and allowed to pass into the bed of ion- exchange material. Eluent flow is then resumed and fractions of eluent are collected at regular intervals from the column outlet. Open column ion-exchange chromatography is very slow due to low eluent flow-rates. Increasing flow rate may result in deteriorated separation efficiency (Figure 3). In modern ion-exchange chromatography the usage of high efficiency ion exchange materials combined with flow-through detection have overcome of these challenges. Separations are performed on the column which is filled with ion-exchanger as particles in uniform size. The particles of ion-exchange material are generally very much smaller than those used for classical open column ion-exchange chromatography [1]. However ion-exchange resins used in modern chromatography have lower capacity than older resins [10]. The eluent must be pumped through the column due to the small particle size of stationary phase. The sample mixture is applied into eluent by the injection port. Finally the separated ions are detected with a flow-through detection instrument [1].
This technique has been used for the analyses of anions and cations, including metal ions, mono- and oligosaccharides, alditols and other polyhydroxy compounds, aminoglycosides (antibiotics), amino acids and peptides, organic acids, amines, alcohols, phenols, thiols, nucleotides and nucleosides and other polar molecules. It has been successfully applied to the analysis of raw materials, bulk active ingredients, counter ions, impurities, and degradation products, excipients, diluents and at different stages of the production process as well as for the analysis of production equipment cleaning solutions, waste streams, container compatibility and other applications [2]. Wide applicability including high performance and high-throughput application formats, average cost, powerful resolving ability, large sample handling capacity and ease of scale-up as well as automation allow the ion exchange chromatography has become one of the most important and extensively used of all liquid chromatographic technique [11].
Although the extensive use of ion exchange chromatography the mechanism of the separation has not completely been elucidated. A considerable effort has been made to describe the ion exchange process theoretically [3,9]. One of the important disadvantages of this technique is that this method provides no direct information on events occurring at the surface of the stationary phase, because the ion-exchange equilibrium is always determined by the balance between the solute interaction and the eluent interaction with the active sites of resin [3]. Ion exchange is similar to sorption, since in both cases a solid takes up dissolved sample. The most important difference between them is in stoichiometric nature of ion exchange. Each ion removed from the solution is replaced by an equivalent amount of another ion of the same charge, while a solute is usually taken-up non-stoichiometrically without being replaced in sorption [15]. Stoichiometric displacement based on the mass action law and describes the retention of a solute ion as an exchange process with the counter ion bound to the surface [9]. According to this model, the retention of a protein under isocratic, linear conditions is related to counter ion concentration and can be represented by equilibrium as follow;
k is the retention factor and Cm is the concentration of the counter ion in the mobile phase. Zp/Zs (= Z) is the ratio of the characteristic charge of the protein to the value of the counter ion and presents a statistical average of the electrostatic interactions of the protein with the stationary phase as it migrates through the column. The behavior of ion exchange chromatographic system can be explained by stoichiometric models. However, the mechanism of the ion exchange separation is more complex and stiochiometric consideration is inapplicable to long-range mechanisms, such as electrostatic interactions due to the distribution of ions in solution is also influenced by the electrostatic potential [3,6]. Other interactions between solute-solute, solute-solvent and solvent-solvent also contribute to retention and selectivity in ion exchange. For example ion-dipole and dispersion interaction, should be included as important mechanisms. Additionally entropic contribution originating from solvent, such as water, structures around ion exchange sites should also be regarded as important [3]. In addition to these the primary separation mechanism is the electrostatic interaction between ion-exchange sites and counter ions in ion exchange chromatography [6].
An important feature differentiating the ion exchange resins from other types of gels is the presence of functional groups. The groups are attached to the matrix. The ion exchange process between the ions in the solution takes place on these functional groups. The exchange of ions between the ion exchange resin and the solution is governed by two principles:
The process is reversible, only rare exceptions are known
The exchange reactions take place on the basis of equivalency in accordance with the principle of electro neutrality. The number of milimoles of an ion sorbed by an exchange should correspond to the number of milimoles of an equally charged ion that has been released from the ion exchange [16].
Equilibrium is established for each sample component between the eluent and stationary phases when a sample is introduced into the ion-exchange chromatography. The distribution of component (A) between the two phases is expressed by the distribution coefficient, "DA".
The value of DA is dependent on the size of the population of molecules of component A in the stationary and eluent phases [1]. As the equilibrium is dynamic, there is a continual, rapid interchange of molecules of component A between the two phases. The fraction of time, fm, that an average molecule of A spends in the mobile phase is given by:
fm = Amount of A in the mobile phase / Total amount of A
fm = [A]m Vm / [A]m Vm + [A]r w
= 1/ 1+ DA (w / Vm)
k' = DA (W / Vm)
fm = 1 / 1 + k'
w: Weight of the stationary phase
Vm: Volume of the mobile phase [1]
The mechanism of the anion and cation exchange are very similar. When analytes enter to the ion exchange column, firstly they bind to the oppositely charged ionic sites on the stationary phase through the Coulombic attraction [2]. In accordance with Coulomb's law, the interactions between ions in the solute and oppositely charged ligands on the matrix in ion-exchange chromatography are due to the electrostatic forces. Coulomb's law is given by the equation as follow;
f: Interaction electrostatic force
q1q2: The charge on ions
: Dielectric constant of the medium
r: The distance between charges.
If the charges on both ions are same (both are positive or negative) the force is repulsive, if they are different (one positive and the other negative) the force is attractive. When the ion charge of the species increase (Divalent ion should interact more strongly than a monovalent ion) and when the dielectric constant decrease (Two oppositely charged molecules increased more strongly in an organic solvent than in water), the interactions increase. On the other hand the distance between the charges increases the interactions decrease. Additionally, other interactions, especially, van der Waals forces participate to the Coulombic forces [2,17].
Ion exchange chromatography, which is also known as adsorption chromatography, is a useful and popular method due to its;
high capacity,
high resolving power,
mild separation conditions,
versatility and widespeared applicability,
tendency to concentrate the sample
relatively low cost [17].
General components of an ion-exchange chromatography are presented as below (Figure 4).
A high pressure pump with pressure and flow indicator, to deliver the eluent
An injector for introducing the sample into the eluent stream and onto the column
A column, to separate the sample mixture into the individual components
An oven, optional
A detector, to measure the analyte peaks as eluent from the column
A data system for collecting and organizing the chromatograms and data
In ion-exchange chromatography, adsorption and desorption processes are determined by the properties of the three interacting entities;
The stationary phase,
The constituents of the mobile phase
The solute [18].
1.2. Stationary phase
Selection of a suitable ion-exchange matrix probably is the most important in ion exchange protocol and is based on various factors such as; ion exchanger charge/strength, linear flow rate/sample volume and sample properties [11]. In ion-exchange chromatography, numerous stationary phases are available from different manufacturers, which vary significantly in a number of chemical and physical properties [6,18]. Stationary phases comprised of two structural elements; the charged groups which are involved in the exchange process and the matrix on which the charged groups are fixed [18]. Ion exchangers are characterized both by the nature of the ionic species comprising the fixed ion and by the nature of the insoluble ion-exchange matrix itself [1].
Ion exchangers are called cation exchangers if they have negatively charged functional groups and possess exchangeable cations. Anion exchangers carry anions because of the positive charge of their fixed groups [15]. The charged groups determine the specifity and strength of protein binding by their polarity and density while the matrix determines the physical and chemical stability and the flow characteristics of the stationary phase and may be responsible for unspecific binding effects [18].
General structure (fibrous or beaded form), particle size and variation, pore structures and dimensions, surface chemistry (hydrophilic or hydrophobic), swelling characteristics of matrix are important factors which effect chromatographic resolution [11,18]. Porosity of ion exchange beads can be categorized as non-porous, microporous and macroporous. (Figure 5 and Figure 6) [14]. High porosity offers a large surface area covered by charged groups and so provides a high binding capacity [13]. However when compared with beaded matrix fibrous ion exchangers based on cellulose exhibit lower chromatographic resolution [14]. On the other hand high porosity is an advantage when separating large molecules [13] and prefractionation [14]. Non-porous matrices are preferable for high resolution separations when diffusion effects must be avoided [13]. Micropores increase the binding capacity but cause to a band broadening. Another disadvantage of microporous beads is that protein can bind to the surface of the beads near to the pores, so penetration of proteins into the pores can prevent or slow down. These problems are overcome by using macroporous particles with pore diameters of about 600-800 nm which are introduced recently. These kinds of particles behave differently compared to microporous materials with respect to microflow characteristics the new term perfusion chromatography has been created [14].
Furthermore a new matrix type which has been recently introduced is based on a completely new principle and exhibits improved chromatographic features when compared with conventional ion exchangers. This matrix which is known as continuous bed does not consist of ion exchange beads or fibers. The matrix is synthesized in the column by polymerization and established from continuous porous support consisting of a nodule chains (Figure 7). The advantages of that matrix are mainly due to the more homogeneous mobile phase flow and short diffusion distances for the proteins. This is explained by the non-beaded form and the unique pore structure of the support [14].
Size, size distribution and porosity of the matrix particles are the main factors which affect the flow characteristics and chromatographic resolution. Small particles improved chromatographic resolution. Stationary phases with particle of uniform size are superior to heterogenous materials with respect to resolution and attainable flow rates. The pore size of ion exchange bead directly effect the binding capacity for a particular protein dependent on the molecular weight of the protein because it determines the access of proteins to the interior of the beads. Binding of large proteins can be restricted to the bead surface only so that the total binding capacity of the ion exchanger is not exploited Pore diameter of 30 nm is optimal for proteins up to a molecular weight of about 200.000 Da [14].
In order to minimize non-specific interactions with sample components inert matrix should be used. High physical stability provides that the volume of the packed medium remains constant despite extreme changes in salt concentration or pH for improving reproducibility and avoiding the need to repack columns. High physical stability and uniformity of particle size facilitate high flow rates, particularly during cleaning or re-equilibration steps, to improve throughput and productivity [13]. There are pH and pressure limits for each stationary phases. For example pH values higher than 8 should not used in silica based materials which are not coated with organic materials. Matrix stability also should be considered when the chemicals such as organic solvents or oxidizing agents should be required to use or when they are chosen for column cleaning [14].
Matrices which are obtained by polymerization of polystyrene with varying amounts of divinylbenzene are known as the original matrices for ion exchange chromatography. However these matrices have very hydrophobic surface and proteins are irreversibly damaged due to strong binding. Ion exchangers which are based on cellulose with hydrophilic backbones are more suitable matrices for protein separations. Other ion exchange matrices with hydrophilic properties are based on agarose or dextran [14].
Several matrix types and their important properties can be listed as follow;
Matrix materials;
Cellulose; Hydrophilic surface, enhanced stability by cross-linking, inexpensive
Dextran; Considerable swelling as a function of ionic milieu, improved materials by cross-linking)
Agarose; Swelling is almost independent of ionic strength and pH, high binding capacity obtained by production of highly porous particles
Polyacrylamide; Swelling behavior similar to dextran
Acrylate-copolymer; High pH stability
Polystyrene-divinilybenzene; Hydrophobic surface, low binding capacity for proteins
Coated polystyrene-divinilybenzene; Hydrophilic surface
Silica; Unstable at pH > 8, rigid particles
Coated Silica; Hydrophilic surface [14]
In addition to electrostatic interactions between stationary phase and proteins, some further mechanisms such as hydrophobic interactions, hydrogen bonding may contribute to protein binding. Hydrophobic interactions especially occur with synthetic resin ion exchangers such as which are produced by copolymerization of styrene and divinylbenzene. These materials are not usually used for separation of proteins. However new ion exchange materials that consist of styrene-divinylbenzene copolymer beads coated with hydrophilic ion exchanger film were introduced. According to the retention behavior of some proteins, it is considered that coating of the beads so efficient that unspecific binding due to hydrophobic interactions cannot be observed. Silica particles have also been coated with hydrophilic matrix. Acrylic acid polymers are also used for the protein separation in ion exchange chromatography. These polymers are especially suitable for purification of basic proteins [14].
The functional groups substituted onto a chromatographic matrix determine the charge of an ion exchange medium; positively-charged anion exchanger or a negatively-charged cation exchanger [13]. Both exchangers can be further classified as strong and weak type as shown in Table 1. The terms weak and strong are not related to the binding strength of a protein to the ion exchanger but describe the degree of its ionization as a function of pH [14]. Strong ion exchangers are completely ionized over a wide pH range, while weak ion exchangers are only partially ionized a narrow pH range [1,11]. Therefore with strong ion exchangers proteins can adsorb to several exchanger sites. For this reason strong ion exchangers are generally used for initial development and optimization of purification protocols. On the other hand weak ion exchangers are more flexible in terms of selectivity and are a more general option for the separation of proteins that retain their functionality over the pH 6-9 range as well as for unstable proteins that may require mild elution conditions [11]. Alkylated amino groups for anion exchangers and carboxy, sulfo as well as phosphato groups for cation exchangers are the most common functional groups used on ion exchange chromatography supports [14]. Sulfonic acid exchangers are known as strong acid type cation exchangers. Quaternary amine functional groups are the strong base exchangers whereas less substituted amines known as weak base exchangers [1]. Number and kind of the substituents are determined the basicity of amino-groups. Immobilized tertiary and quaternary amines proved to be useful for ion exchange chromatography. Immobilized diethylaminoethyl and carboxymethyl groups are the most widely used ion exchangers [11].
The ion exchange capacity of an ion-exchanger is determined by the number of functional groups per unit weight of the resin [13]. The total ionic capacity is the number of charged functional groups per ml medium, a fixed parameter of each medium and can be given as mval/ml for small ions. Density and accessibility of these charged groups both on the surface and within the pores define the total binding capacity. Ionic medium and the presence of other proteins if a particular protein is considered also affect the binding capacity. However, under defined conditions, the amount of the certain protein which is bound to ion exchanger is more suitable parameter for determining and comparing the capacity of ion exchange chromatography. Albumin for anion exchangers and hemoglobin for cation exchangers is usually used for this purpose. Determination of the binding capacity before the experiment is generally recommended because the capacity for a particular protein depends on its size and also on the sample composition. The binding capacity of a column can be increased for proteins which are retained on the column at high salt concentrations. The salt concentration is adjusted to a suitable concentration in which the protein of interest tightly bound to the ion exchanger while others which have lower affinity pass through the column without occupying binding sites [14].
1.3. Mobile phase (Eluent)
In ion exchange chromatography generally eluents which consist of an aqueous solution of a suitable salt or mixtures of salts with a small percentage of an organic solvent are used in which most of the ionic compounds are dissolved better than in others in. Therefore the application of various samples is much easier [1,3]. Sodium chloride is probably the most widely used and mild eluent for protein separation due to has no important effect on protein structure. However NaCl is not always the best eluent for protein separation. Retention times, peak widths of eluted protein, so chromatographic resolution are affected by the nature of anions and cations used. These effects can be observed more clearly with anion exchangers as compared to cation exchangers [14]. The salt mixture can itself be a buffer or a separate buffer can be added to the eluent if required. The competing ion which has the function of eluting sample components through the column within reasonable time is the essential component of eluting sample. Nature and concentration of the competing ions and pH of the eluent are the most important properties affecting the elution characteristics of solute ions [1].
The eluent pH has considerable effects on the functional group which exist on the ion exchange matrix and also on the forms of both eluent and solute ions. The selectivity coefficient existing between the competing ion and a particular solute ion will determine the degree of that which competing ion can displace the solute ion from the stationary phase. As different competing ions will have different selectivity coefficients, it follows that the nature of competing ion will be an important factor in determining whether solute ions will be eluted readily. The concentration of competing ion exerts a significant effect by influencing the position of the equilibrium point for ion-exchange equilibrium. The higher concentration of the competing ion in the eluent is more effectively displace solute ions from the stationary phase, therefore solute is eluted more rapidly from the column. Additionally elution of the solute is influenced by the eluent flow-rate and the temperature. Faster flow rates cause to lower elution volumes because the solute ions have less opportunity to interact with the fixed ions. Temperature has relatively less impact, which can be change according to ion exchange material type. Enhancement of the temperature increases the rate of diffusion within the ion-exchange matrix, generally leading to increased interaction with the fixed ions and therefore larger elution volumes. At higher temperatures chromatographic efficiency is usually improved [1].
Eluent degassing is important due to trap in the check valve causing the prime loose of pump. Loss of prime results in erratic eluent flow or no flow at all. Sometimes only one pump head will lose its prime and the pressure will fluctuate in rhythm with the pump stroke. Another reason for removing dissolved air from the eluent is because air can get result in changes in the effective concentration of the eluent. Carbon dioxide from air dissolved in water forms of carbonic acid. Carbonic acid can change the effective concentration of a basic eluent including solutions of sodium hydroxide, bicarbonate and carbonate. Usually degassed water is used to prepare eluents and efforts should be made to keep exposure of eluent to air to a minimum after preparation. Modern inline degassers are becoming quite popular [10].
For separation the eluent is pumped through the system until equilibrium is reached, as evidenced by a stable baseline. The time required for equilibrium may vary from a couple of minutes to an hour or longer, depending on the type of resin and eluent used [10]. Before the sample injection to the column should be equilibrated with eluent to cover all the exchange sites on the stationary phase with the same counter ion. When the column is equilibrated with a solution of competing ion, counter ions associated with the fixed ions being completely replaced with competing ions. In this condition the competing ions become the new counter ions at the ion exchange sites and the column is in the form of that particular ion [1].
Isocratic elution or gradient elution can be applied for elution procedure. A single buffer is used throughout the entire separation in isocratic elution. Sample components are loosely adsorbed to the column matrix. As each protein will have different distribution coefficient separation will achieved by its relative speeds of migration over the column. Therefore in order to obtain optimum resolution of sample components, a small sample volume and long exchanger column are necessary. This technique is time consuming and the desired protein invariably elutes in a large volume. However no gradient-forming apparatus is required and the column regeneration is needless. Alteration in the eluent composition is needed to achieve desorption of desired protein completely. To promote desired protein desorption continuous or stepwise variations in the ionic strength and/or pH of the eluent are provided with gradient elution. Continuous gradients generally give better resolution than stepwise gradients [11].
Additives which are protective agents found in the mobile phase are generally used for maintain structure and function of the proteins to be purified. This is achieved by stimulating an adequate microenvironment protection against oxidation or against enzymatic attacks [14]. Any additives used in ion exchange chromatography, should be checked for their charge properties at the working pH in order to avoid undesired effects due to adsorption and desorption processes during chromatography [13-14]. It is recommended to include in the elution buffer those additives in a suitable concentration which have been used for stabilization and solubilization of the sample. Otherwise precipitation may occur on the column during elution [14]. For example; zwitterionic additives such as betaine can prevent precipitation and can be used at high concentrations without interfering with the gradient elution. Detergents are generally useful for solubilization of proteins with low aqueous solubility. Anionic, cationic, zwitterionic and non-ionic (neutral) detergents can be used during ion exchange chromatography. Guanidine hydrochloride or urea, known as denaturing agents can be used for initial solubilization of a sample and during separation. However, they should use if there is a requirement. Guanidine is a charged molecule and therefore can participate to the ion exchange process in the same way as NaCl during separation process [13].
Commonly used eluent additives which have been successfully used in ion exchange chromatography can be given as follow;
EDTA; Ethylenediamine tetraacetic acid
Polyols; Glycerol, glucose, and saccharose
Urea and guanidinium chloride
Organic solvents
Sulfhydryl reagents
Protease inhibitors [14]
1.4. Buffer
In ion exchange chromatography, pH value is an important parameter for separation and can be controlled and adjusted carefully by means of buffer substances [18]. In order to prevent variation in matrix and protein net charge, maintenance of a constant mobile phase pH during separation is essential to avoid pH changing which can occur when both protein and exchanger ions are released into the mobile phase [11]. By means of buffer substances pH value can be controlled and adjusted. Concentration of H+ and the buffering component influence the protein binding to the stationary phase, chromatographic resolution and structural as well as functional integrity of the protein to be separated. Thus a suitable pH range, in which the stability of sample is guaranteed, has to be identified. Keeping of the sample function is related with the preservation of its three dimensional structure as well as with its biological activity [18]. A number of buffers are suitable for ion-exchange chromatography. A number of important factors influences the selection of mobile phase including buffer charge, buffer strength and buffer pH [11]. Properties of good buffers are high buffering capacity at the working pH, high solubility, high purity and low cost. The buffer salt should also provide a high buffering capacity without contributing much to the conductivity and should not interact with the ion exchanger functional groups as well as with media [11,17]. The buffering component should not interact with the ion exchanger because otherwise local pH shifts can occur during the exchange process which may interfere the elution. Interactions with stationary phase as well as with additives of the mobile phase and with subsequent procedures may be occur with buffer component and selected pH range. Precipitation of the mobile phase components can be observed for example when phosphate buffer and several di- and trivalent metal ions such as Mg+2 and Ca+2 are mixed or when anionic detergents (i.e. cholate) are used under acidic conditions or in the presence of multivalent metal ions. Precipitation of metal oxides and hydroxides can occur under alkaline conditions. Buffer components may also affect enzymatic assays used for screening and analysis of chromatography fractions [14]. The concentration of buffer salts usually ranges from 10 to 50 mM. Commonly used buffers are presented in Table 2 and Table 3 for cation and anion exchange chromatography [17].
Generally, applications of ıon exchange chromatography are performed under slightly acidic or alkali conditions, pH range 6.0-8.5 but there are also more acidic and more alkali buffers. Additionally the buffering component should not act as an eluting ion by binding to the ion exchanger. Anionic buffer component such as phosphate or MOPS in cation exchange chromatography and cationic buffers such as ethanolamine, Tris and Tricine in anion exchange chromatography are recommended. Besides interactions of buffer component with stationary phase, there are also possible interactions with additives of the mobile phase. To achieve sufficient buffer capacity the pKa of the buffer component should be as close to the desired pH value as possible difference no more than ± 0.5 pH units. However there are examples of successful separations at which the buffering capacity is very low [17-18]. It has to be considered that the pKa is a temperature dependent value. Performing on ion exchange separation with the same elution buffer at room temperature or in the cold room can have a remarkable effect on the buffer capacity. For optimal binding of a sample ion to an ion-exchanger the ionic strength and thus also the buffer concentrations has to be low in sample and equilibration buffers [18].
1.5. Detection
Conductivity detector is the most common and useful detector in ion exchange chromatography. However UV and other detectors can also be useful [10]. Conductivity detection gives excellent sensitivity when the conductance of the eluted solute ion is measured in an eluent of low background conductance. Therefore when conductivity detection is used dilute eluents should be preferred and in order for such eluents, to act as effective competing ions, the ion exchange capacity of the column should be low [1].
Although recorders and integrators are used in some older systems, generally in modern ion exchange chromatography results are stored in computer. Retention time and peak areas are the most useful information. Retention times are used to confirm the identity of the unknown peak by comparison with a standard. In order to calculate analyte concentration peak areas are compared with the standards which is in known concentration [10].
Direct detection of anions is possible, providing a detector is available that responds to some property of the sample ions. For example anions that absorb in the UV spectral region can be detected spectrophotometrically. In this case, an eluent anion is selected that does not absorb UV. The eluent used in anion chromatography contains an eluent anion, E-. Anions with little or no absorbance in the UV spectral region can be detected spectrophotometrically by choosing a strongly absorbing eluent anion. An anion with benzene ring would be suitable [10]. Usually Na+ or H+ will be the cation associated with E-. The eluent anion must be compatible with the detection method used. For conductivity the detection E should have either a significantly lower conductivity than the sample ions or be capable of being converted to a non-ionic form by a chemical suppression system. When a spectrophotometric detection is employed, E will often be chosen for its ability to absorb strongly in the UV or visible spectral region. The concentration of E- in the eluent will depend on the properties of the ion exchanger used and on the types of anions to be separated [10].
2. Ion exchange chromatograpy applications
Ion exchange chromatography can be applied for the separation and purification of many charged or ionizable molecules such as proteins, peptides, enzymes, nucleotides, DNA, antibiotics, vitamins and etc. from natural sources or synthetic origin. Examples in which ion exchange chromatography was used as a liquid chromatograpic technique for separation or purification of bioactive molecules from natural sources can be given as below.
3. Conclusion
Since the isolation of pharmacologically active substances which are responsible for the activity became possible at the beginning of the 19th century drug discovery researches have increased dramatically [33]. Therefore within the last decade there has also been increasing interest in the liquid chromatographic processes because of the growing pharmaceutical industry and needs from the pharmaceutical and specialty chemical industries for highly specific and efficient separation methods. Several different types of liquid chromatography techniques are utilized for isolation of bioactive molecules from different sources [25]. Ion exchange chromatography is probably the most powerful and classic type of liquid chromatography. It is still widely used today for the analysis and separation of molecules which are differently charged or ionizable such as proteins, enzymes, peptides, amino acids, nucleic acids, carbohydrates, polysaccharides, lectins by itself or in combination with other chromatographic techniques [34]. Additionally ion exchange chromatography can be applied for separation and purification of organic molecules from natural sources which are protonated bases such as alkaloids, or deprotonated acids such as fatty acids or amino acid derivatives [35]. Ion exchange chromatography has many advantages. This method is widely applicable to the analysis of a large number of molecules with high capacity. The technique is easily transferred to the manufacturing scales with low cost. High levels of purification of the desired molecule can be achieved by ion exchange step. Follow-up of the nonsolvent extractable natural products can be realized by this technique [17,35]. Consequently ion exchange chromatography, which has been used in the separation of ionic molecules for more than half a century is still used as an useful and popular method for isolation of natural products in modern drug discovery and it continue to expand with development of new technologies.


text:
Design Project Preparation
EDD5104 is rated by StudentVIP members:
rate me!
0 StudentVIP members in EDD5104
0 textbooks listed
0 tutors available
4 tutor searches
0 subject ratings
What do you rate EDD5104?
Add EDD5104 to your subjects
You can add EDD5104 to your StudentVIP account to find textbooks, tutors and more.Join StudentVIP
Reviews and tips for EDD5104
0 reviews
Where are classes for EDD5104?
Easy, get a great map app for Edith Cowan Uni., including locations for classes in EDD5104.Get Lost On Campus
0 notes available for EDD5104
Upload & earn:Sell your notes
Tutors for EDD5104
0 tutors available for tutoring EDD5104Become a tutor for EDD5104
4 tutor searches for EDD5104!
Encourage students to become a tutor. Add a no-obligation tutor request. We'll notify you when a new tutor registers.


text:
After more than a month long hiatus, I am finally getting back to blogging. Several weeks ago I saw a recipe for English muffins I wanted to try, and figured it would be fitting to make them during the Olympics. Like the rest of the world I became fascinated with everything Olympics for two weeks, and the realization that they are for some nothing more than a two week international orgy did nothing to quell my interest. I of course got swept up in watching sports that would otherwise never grace American television (handball and water polo are awesome) and in that forgot completely about making these.
Pretty much immediately after the closing ceremonies I was in full on crazy-apartment-move-mode, frantically packing things and cooking minimally. Once I moved into the new place I was excited to test out the oven, and then promptly got sick and did nothing but eat soup from a can for 7 days. Finally I baked up a storm (brioche, calzones, baguettes, and English muffins) Labor Day weekend.
These muffins were the perfect way to start of the carb-baking extravaganza because they were quick (less than 4 hours total, maybe 30-45 minutes of actual work) and didn't require me to turn on the oven (cooked in a stovetop pan which I did not know) when it was pushing 90 degrees outside.
In a bowl mix together your yeast, sugar, salt, and 1.5 cups of flour. Add in the butter and milk and mix until the ingredients have combined well.
Gradually add the rest of the flour (I ended up needing 2 3/4 cups total) until you have a soft dough ball that clears the sides of your mixing bowl. Knead by hand for 5 minutes (or in a mixer for 2) and then place in a lightly oiled bowl to rise for an hour.
I generally have a tendency to add more flour than necessary, but it's important to add as little as possible once you've reached the dough consistency you want. Any more will lead to overly dry and tough muffins.
After your dough has risen, punch it down and let it rise another hour. Place your risen dough onto a floured surface and roll it out. You should roll it to about 3/4 inch thickness. I got a little too rolling pin happy and probably caused mine to be a bit flat.
Using a cup, cookie cutter, or anything round, cut out circles of dough and place onto a pan covered in corn meal (sprinkle more over the top of them). When you can't cut more circles ball up the dough, roll it back out, and repeat. You should make around 10, so when I had 15 I figured I had rolled the dough a bit too much.
Let your muffins rise for another 45 minutes, toward the end of that rise lightly oil a pan and heat it over low-medium heat (a bit more towards medium).
Cook muffins in the heated pan, flipping halfway through to make sure each side gets nice and brown. They should take about 7 minutes per side.
Let cool 15 minutes before slicing. These also freeze very well.
English Muffins
- 3 cups AP flour
- 1 teaspoon yeast
- 1 tablespoon sugar
- 1/2 cup milk
- 1/2 cup water
- 2 tablespoons butter
- 3/4 teaspoon salt
- Cornmeal for dusting (about 1/4 cup)
In a mixing bowl combine yeast, sugar, 1.5 cups flour, salt, milk, butter, and water.
Mix until all combined, then gradually add remaining flour until a solid dough ball forms. Do not continue to add flour once this has happened (you may not need all 3 cups).
Place dough in a lightly oiled bowl, cover, and let rise for 45 minutes. Punch down and let rise for another 45 minutes after.
Roll dough out on a lightly floured surface to 3/4 inch thick, and using a cup or cookie cutter cut out circular muffins. Place on a pan dusted with corn meal. Ball up remaining dough, roll out again, and continue to cut out muffins until all dough is used up.
Let muffins rise for 45 minutes. Preheat lightly oiled pan over low-medium heat, and cook muffins in pan, allowing 7 minutes per side. Cool 15 minutes before slicing.


text:
Everyday we get the opportunity to build great products and few weeks ago we build some wakeboards for Germaine Marine in Arizona. So if your in the area, head on over and pick one up, it's a great way to support two U.S. businesses!
If you have a boat shop and are interested in our shop board programs, give us a call and lets see how we can help you out!
Here are a few other pics of custom wakeboards we have done:


text:
Mike Simpson may have won a tough primary election, but he still has much to answer for, writes Beverly Beach.
Congressman Mike Simpson touts his "accomplishments," but fails to explain how those accomplishments benefit Idaho. Our Idaho congressional delegation - Simpson, Sens. Jim Risch and Mike Crapo and Rep. Raul Labrador - has forgotten who they represent.
Until recently, Idaho had the highest percentage of minimum wage jobs in the nation. To me, that is absolutely unacceptable. You would not work to raise the wages of those making only $7.25 an hour, Congressman Simpson? Surely you understand that putting extra money in the pocket of low-paid workers would buy food, gas, clothing and other necessities. Those purchases would stimulate the local economy, creating Idaho jobs.
Why have you never sponsored a bill that would levy a higher tariff on Chinese goods being imported into America? U.S. companies cannot compete with the low wages paid Chinese workers. Our products are already too expensive for the average Chinese consumer, yet the Chinese government adds a 25 percent tariff to discourage the purchase of American goods. We need to return the favor, as our present 2.5 percent tariff on imported Chinese goods makes for an unfair trade balance.
Why have you not sponsored a bill that would place tariffs on goods produced outside the United States by U.S. companies, Congressman Simpson? There is no reason other than greed that a U.S. company should have production plants outside the country for goods sold within the U.S. Outsourcing costs America millions of jobs.
What have you done to assist the thousands of Idahoans who have lost their houses to greedy bankers, Congressman Simpson? Have you taken it upon yourself to understand the real causes of the housing bubble that collapsed and cost millions of Americans their homes? Congress bailed out the banks but did nothing to help those homeowners who were literally scammed by the banks that were "too big to fail." I am sure you realize funds for Idaho pensions were lost through the preying upon pension funds all over the U.S. by the banks and recklessness of high-risk bank trading. Will you support bringing back Glass-Steagall?
By voting to repeal the Affordable Care Act 40 times, you wasted taxpayer money, Congressman Simpson. Where were your solutions to America's healthcare problems? Did those 40 votes accomplish anything other than playing partisan politics? What have you done to help those Idahoans who are in need insurance but can't get it because Idaho refused to expand Medicaid?
Simpson's vote to repeal the estate tax has absolutely no bearing on the vast majority of Idahoans. Only estates valued at more than $5 million for a single person are required to pay the so-called "death tax." Nationwide, only one tenth of one percent of estates are affected by this repeal.
We could also address continuous threats to cut Social Security and Medicare, high interest on student loans and credit cards, job creation and government shutdowns, but that is another column.


text:
Global Stocks Climb to 6-Year High on IMF, Tech Rally
Global stocks rallied to the highest level in almost six years as Apple Inc. (AAPL) jumped and the International Monetary Fund indicated it would raise its outlook for the American economy.
The MSCI All-Country World Index rose 0.6 percent at 4 p.m. in New York, the highest closing since January 2008. The Standard & Poor's 500 Index increased 0.5 percent to a record. The Nasdaq Composite Index (CCMP) surged 1.1 percent as technology stocks rallied. Natural gas touched the highest level since July 2011 on speculation over a cold start to the new year. China's seven-day repurchase rate was the highest since June 20 and the yuan closed at the most since 1993. Futures contracts on Australia's S&P/ASX 200 Index climbed 0.5 percent as of 5:22 p.m. New York time.
IMF Managing Director Christine Lagarde said yesterday the organization is raising its outlook for the U.S. economy. Consumer spending rose in November by the most in five months as Americans took advantage of store discounts during the year-end shopping season. Apple jumped 3.8 percent after the company struck a deal to sell its iPhones through China Mobile Ltd. (941), the world's largest phone company. China's money rates surged as banks hoarded cash to meet year-end requirements.
"It's a cauldron of bullish factors," Donald Selkin, who helps manage about $3 billion as the New York-based chief market strategist at National Securities Corp., said by phone. "There's the seasonal factor, the IMF raising its forecast and the Fed saying they're going to keep the federal funds rate low."
Global Rally
Worldwide stocks have rallied 2.5 percent over the past four trading days, boosting gains for 2013 to 19 percent. The Dow jumped 3 percent last week and the S&P 500 climbed 2.4 percent, with both gauges setting records, as the Federal Reserve said it will reduce the pace of bond buying amid faster-than-estimated economic growth. The S&P 500 has advanced 28 percent in 2013, putting it on course for its biggest annual rally since 1997.
The IMF is raising its outlook for the U.S. economy as a budget deal in Washington and the Fed's plan to taper its bond buying ease doubts about the future, Lagarde said yesterday in an interview broadcast on NBC's "Meet the Press." The IMF predicted in October that the world's largest economy would expand 2.6 percent next year. Lagarde didn't set out any new projections.
Economic Data
U.S. household purchases, which account for almost 70 percent of the economy, rose 0.5 percent after a 0.4 percent gain in October that was larger than previously estimated, the Commerce Department reported today in Washington. The median forecast of 76 economists in a Bloomberg survey called for a 0.5 percent rise. Incomes climbed less than forecast, reflecting a slump in earnings by farmers.
A separate report showed consumer confidence increased in December. The Thomson Reuters/University of Michigan final index of consumer sentiment climbed to 82.5 from 75.1 a month earlier. The median forecast of 61 economists in a Bloomberg survey called for 83 after a preliminary reading of 82.5.
"Most of the economic data points suggest stronger growth going forward," Eric Green, director of research and fund manager at Penn Capital Management, said by phone. The Philadelphia-based firm oversees about $7 billion. "This is a very good seasonal period of time for the markets."
December Gains
The S&P 500 has gained 1.2 percent so far this month. December has been the second-best month for U.S. equity returns, according to data compiled by Bloomberg that starts in 1928. The average gain for the month is 1.5 percent, more than twice the overall monthly mean of 0.6 percent. The last December retreat for the S&P 500 was in 2007. U.S. equity exchanges will close early tomorrow, at 1 p.m., before the Christmas holiday.
Technology stocks jumped 1.5 percent as a group in the S&P 500 as Apple ended six years of negotiations, striking a deal that will give both the U.S. phone maker and China Mobile a means to fight declining share in the market of 1.2 billion wireless subscribers. China Mobile will sell the iPhone 5s and 5c models in its stores from Jan. 17, the companies said in a statement that provided no financial terms.
Facebook Inc. surged 4.8 percent as the company began trading as a member of the S&P 500 today. T-Mobile US Inc. rose 2.8 percent after people familiar with the situation said SoftBank Corp. Chief Executive Officer Masayoshi Son is exploring a deal for Sprint Corp. to buy the majority of the wireless-phone provider next year. Micron Technology Inc. slid 3.1 percent after Bank of America Corp. downgraded its rating.
Technology Rally
Today's rally in technology shares helped the Nasdaq Composite surpass 4,120, a level that represents a recovery of 76.4 percent of the index's decline during the bursting of the Internet bubble. The threshold is seen by Fibonacci analysts as the last obstacle for a full recovery. The benchmark gauge, which plunged 78 percent from its peak of 5,048.62, set on March 10, 2000, would need to climb about 22 percent to reclaim its record.
European stocks rose 3.7 percent last week, the biggest jump since April, after the Fed's decision to reduce its monthly bond purchases increased investors' confidence in the strength of the U.S. economic recovery. The Stoxx 600 rallied 16 percent this year, heading for its largest annual increase since 2009.
Shares in Europe are poised for a third year of gains in 2014, restoring almost all the losses suffered during the financial crisis, as economic growth overcomes record pessimism on earnings. Equities will rise 12 percent in 2014, the average projection of 18 forecasters tracked by Bloomberg News shows.
Treasury Yields
Yields on five-year U.S. notes rose four basis points to 1.68 percent, reaching a three-month high. Thirty-year bonds advanced, pushing yields down to 3.83 percent, amid wagers inflation will stay in check as the Fed slows asset purchases.
The Bloomberg Dollar Index retreated 0.1 percent. The dollar was little changed at 104.15 yen. It climbed to 104.64 on Dec. 20, the highest since October 2008. Japan's currency slipped 0.1 percent to 142.67 per euro.
China's seven-day repurchase rate, a gauge of funding availability in the banking system, jumped 124 basis points today to 8.84 percent, the highest level since June 20, according to a daily fixing from the National Interbank Funding Center. The rate, which has more than doubled from 4.37 percent in the past week, touched a record 10.77 percent in June.
The yuan advanced 0.02 percent to close at 6.0702 per dollar in Shanghai, the strongest since the government unified the market and official exchange rates at the end of 1993. The People's Bank of China boosted the daily fixing today by 0.06 percent, the most since Dec. 9, to 6.1161 per dollar.
Turkish Stocks
The Borsa Istanbul 100 Index of Turkish shares fell 2.1 percent, extending losses to 9 percent since a corruption investigation targeting Prime Minister Recep Erdogan's government was announced Dec. 17. Emlak Konut CEO Murat Kurum and two board members returned to work yesterday after being questioned as part of the police investigation.
U.S. natural gas advanced 1 percent after earlier climbing to the highest since July 2011. Forecasters including Commodity Weather Group LLC in Bethesda, Maryland, predicted that below-normal temperatures in the central U.S. will spread through the East from Dec. 28 through Jan. 6.
Crude oil dropped 0.4 percent to $98.91 a barrel, retreating from a two-month high.
Gold declined 0.6 percent to $1,197 an ounce on speculation less U.S. stimulus and an improving economy will cut demand for bullion as a protection of wealth. Gold has tumbled 29 percent this year, set for its biggest annual drop since 1981, as some investors lost faith in the metal as a store of value. It climbed the previous 12 years.
To contact the reporters on this story: Nick Taborek in New York at firstname.lastname@example.com; Lu Wang in New York at email@example.com
To contact the editor responsible for this story: Lynn Thomasson at email@example.com


text:
|Adult Education Fair
Event Type: Other
Age Group(s): Adults, Seniors
Date: 2/6/2014
Start Time: 1:00 PM
End Time: 7:00 PM
Learn about higher education, financial aid, and child care options that fit your schedule and your goals, whether you're a single parent, a retiree, or a full-time employee. For details about schools and organizations that will be there, and to register, visit https:/mcadultedfair.eventbrite.com. Registration is encouraged, but not required.Library: Anderson Public Library
Location: Chief Anderson Room


text:
Urdu Columns
Today's Columns
About Us
Contact Us
تازہ تر ین:
Samundar O Nadar Sehraon Se Malaa Maal Balochistan
Nazir Naji
Published in
Recent Column(s)
Dar Sahib Hamare Kitne Hamdard Hain? (Published on 24 March 2018)
Muqadmay Par Muqadma (Published on 22 March 2018)
Siasi Adam Istehkam Ka Ilaj (Published on 21 March 2018)
Aagaya Hamara Shagird (Published on 20 March 2018)
Aik Rupay Mein Steel Mill (Published on 18 March 2018)
comments powered by Disqus.
Find us on Facebook
Archive Columns
Privacy Policy
We InsightPk.com do not store any of your personnel information. We are using third party tool for comments, this third party tool may use the information about sites you have visited to provide services and ads according to your interest. Any information shared with this third party tool is handled according to
privacy policy
of that tool, so we strongly recommend you to agree with their privacy policy before using that tool. We may contain external links that may redirect to third party sites, we strongly recommend to read and agree with privacy policy of those sites before using their services. We are using third party tool for advertisement, these tools may be using information about your recent visited sites for providing quality advertisements. In any case we are not responsible for any loss, distribution or any kind of action that may occur with your shared information. Our privacy policy may change anytime without any intimation. if you choose to use our services, then you agree to our privacy policy.
We InsightPk.com are using content from third parties and we may not own one or more of them. We are just showing content from different newspapers at a common location and we never claim to own any of these collected content. These contents are personnel opinions of authors, it does not reflect our belief and we may disagree from these opinions. Comments on the content are also personnel opinions of commenter, it does not reflect our belief and we may disagree from these opinions. These contents or comments may contain information that may not be suitable for children, single person, more than one person or a community, so we should not be considered responsible in any case. We may contain external links that may lead users to third party websites. We are not responsible for any content shared on those third party websites. We are using third party tools for comments and advertisements. We are not responsible for any advertisement or any other content shown by these tools. Our policies may change anytime without any intimation. If you choose to use our services, then you agree to our policies.


text:
All Fields Required
Privacy Policy
Areas Modeled by Tool and General Definitions
Storage Efficiency
Storage Consolidation
Rapid Application Recovery
Cost effective disaster recovery
* Source : Wikibon
© 2013 NetApp
Privacy Policy |
Contact Us
495 E. Java Drive, Sunnyvale, CA 94089 USA
Note: All results generated by the TCO Calculator are estimates for illustration purposes only and do not represent any guarantee or expectation of performance for a particular customer or the user. In addition, space savings are likely to be affected by a number of factors not included in these calculations. Actual results may vary. Thus, space savings realized in specific customer operating environments will likely vary from those listed above. Customers or users should conduct detailed analyses in order to generate results that reflect the specific circumstances of their storage environments.
This information generated by the TCO Calculator is provided "as is" without warranty of any kind, express or implied, and is based on data provided by Customer or user input or based on product plans that are subject to change by NetApp without notice. NetApp shall not be responsible for any damages arising out of the use of, or otherwise related to, the TCO Calculator. Nothing contained in this report or results of use of the TCO Calculator is intended to create, or shall have the effect of creating any warranties or representations from NetApp or reseller partners authorized by NetApp.


text:
About This Product
Sold by
Size: Water Bottle (24 oz)
Drink more water. Your skin, hair, body, and mind will thank you. And now, drink out of a fully customizable water bottle and your sense of style will thank you as well. Dang, hydration never looked so good!
- 24 oz. bottle.
- Made with 18/8 stainless steel.
- Height: 10.8" Weight: 10 oz.
- 100% BPA free.
- Comes with a threaded lid.
- Lightweight and durable; crack proof, spill proof.
- Hand wash only. Not recommended for dishwasher.
- Does not give beverages a plastic taste.
- Safe for refrigerator, but not freezer.
- Certified free of harmful chemicals.
Will be made by
Pexagon Technology
Branford, CT, United States
About This Design
Run With The Bulls 2018 black water bottle 24oz
This water bottle fits at least 4 consumers: 1) festival bull runners, 2) stock market investors, 3) riders on a motorcycle run, and 4) people with the last name Bull who like to hang out or run. Of course, you might fill all 4 demographics! :) Run With The Bulls is original Steamy Raimon art.
available on 103 products
Artwork designed by
Tucson, AZ, United States
There are no reviews for this product yet.
Showing 1-0 of 0 reviews
Page 1 of 1
Showing 1-0 of 0 reviews
Page 1 of 1
Have you purchased this product? Write a review!
Other Info
Product ID: 256409235360590740
Designed on
Rating: G Report this product


text:
The offseason woes of the New England Patriots have been well documented and highly publicized. There was the disconnect with Wes Welker, the arrest of Aaron Hernandez and the ongoing injury drama of Rob Gronkowski, yet the popular consensus has been that the Patriots would be alright; after all, they still have Tom Brady throwing the ball.
The question has now become, can Brady be enough to maintain New England's status as an NFL elite?
Two weeks into the season, the Patriots are sitting atop the AFC East at 2-0, but the wins have been as much about their opponents' mistakes as it has been about their success. If ever a team could win two games and still be seen as falling off, this is it.
First, the Pats have faced two divisional opponents that were expected to be among the worst teams in the league. Both teams started a rookie quarterback that did not receive a full complement of preseason snaps. Both teams have questionable offensive lines and inconsistent talent at the wide receiver position. Both teams should have been easy wins for the Patriots.
Instead, both teams pushed the Patriots to the very end of the game and New England was lucky to come away with the win.
This is not the team we have seen take up residence in the AFC Championship Game and make going to the Super Bowl look easy. It is not the team we have seen set offensive records and complete near perfect seasons with ease.
Instead, Brady cannot count on a receiver to catch a pass, and the receivers cannot count on Brady to keep his cool. The running game that was so productive last season is now in shambles, and injuries are keeping what talent the team does have from seeing the field. The receiving game is in the hands of Julian Edelman and two rookies the casual fan has never even heard of. Brady's completion percentage has taken a dive, and it has been the defense that has pulled them from the jaws of defeat, instead of the offense making up for a shaky D.
This is definitely not the Patriots we are used to seeing.
The two wins make the Patriots' struggles easier to fathom, but if you watch Brady during his post game interviews without knowing the scores, you would swear his team had lost.
While the Patriots have barely been able to beat two of the weaker teams in the league, the Denver Broncos and San Francisco 49ers have looked like they are in mid-season form, both sending potential Super Bowl contenders away with a loss. Compare these games to what we have seen from New England and it easy to see that the Patriots are no longer on the same level as the NFL elite. If Brady and his young receivers can get on the same page and make it click, maybe they can return to AFC dominance, but no one is going to recommend that fans hold their breath.
It appears as though the impossible has finally happened. Tom Brady is no longer super human, and the Patriots are no longer the AFC favorite. How they will respond will be interesting to see.
Jeff Everette covers the Miami Dolphins, for RantSports.com. You can follow him on Twitter @jeverettesports, "like" his page on Facebook, "Trust" him on Sulia, or join his circles on Google.
Rob Gronkowski Can't Hurry Back Fast Enough For Depleted New England Patriots
Julian Edelman Is Not Permanent Solution For New England Patriots
Rex Ryan Deserves To Get Fired, Pay Mark Sanchez


text: KDL-52XBR7 was all the rage upon its arrival, promising slick visuals and a dejudder processor that would wow, stun and awe. Unfortunately, it seems the set hasn't exactly lived up to expectations, as the deep black levels, accurate color temperature and color decoding, comprehensive complement of inputs and beautiful body weren't enough to overcome the breathtaking $4,200 price tag. Furthermore, the 240Hz refresh rate was found to offer "only minor improvements to picture quality," proving our fears of it being more about marketing than performance absolutely correct. Bottom line? Take your dollars elsewhere -- chances are, you won't miss the Hz.


text:
The sun will make an early exit Wednesday.
The National Weather Service forecasts an 80 percent chance of rain Wednesday. The rain should begin after 10 a.m. The high temperature should be 47 degrees.
There will be a 50 percent chance of rain Wednesday night, and a low temperature of 42 degrees.
Expect rain through the rest of the week.


text: Alberto Mielgo, a brilliant art director, worked on the first minute of this Beatles Rock Band video. The character design and animation was the work of the very talented Rob Valley, who has an incredible ability to distort things. The video is already two years old, but I can not resist watching it from times to times. It is incredible to see how good the design is, how sharp, controlled and meaningful each choice of colour is.


text:
Lions DT Ndamukong Suh was the first pick of day one of the Pro Bowl draft.
Seahawks signed DT Tom Johnson, formerly of the Vikings, to a one-year, $2.7 million contract.
RG Joe Berger announced his retirement after 13 NFL seasons.
Free agent CB Marcus Cooper is visiting the Cardinals on Friday.
The Redskins have withdrawn their offer to free agent OLB Junior Galette.
Jets agreed to terms with WR Terrelle Pryor, formerly of the Redskins.
Eagles SLB Mychal Kendricks is recovering from "clean-up" ankle surgery.
The Los Angeles District Attorney's office has dropped vandalism charges against Bills WR Zay Jones.
Free agent WR Jordan Matthews visited the Packers on Thursday.
Eagles signed WR Mike Wallace to a one-year contract.
Raiders signed OT Breno Giacomini, formerly of the Texans.
Packers signed CB Tramon Williams, formerly of the Cardinals.


text:
What does voider mean?
Definitions for voider
Here are all the possible meanings and translations of the word voider.
Princeton's WordNet
invalidator, voider, nullifier(noun)
an official who can invalidate or nullify
"my bank check was voided and I wanted to know who the invalidator was"
defecator, voider, shitter(noun)
a person who defecates
voider, gusset(noun)
a piece of chain mail covering a place unprotected by armor plate
clothes hamper, laundry basket, clothes basket, voider(noun)
a hamper that holds dirty clothes to be washed or wet clothes to be dried
One who, or that which, voids, empties, vacates, or annuls.
Webster Dictionary
one who, or that which, voids, /mpties, vacates, or annuls
a tray, or basket, formerly used to receive or convey that which is voided or cleared away from a given place; especially, one for carrying off the remains of a meal, as fragments of food; sometimes, a basket for containing household articles, as clothes, etc
a servant whose business is to void, or clear away, a table after a meal
one of the ordinaries, much like the flanch, but less rounded and therefore smaller
Anagrams for voider »
Chaldean Numerology
The numerical value of voider in Chaldean Numerology is: 7
Pythagorean Numerology
The numerical value of voider in Pythagorean Numerology is: 1
Images & Illustrations of voider
Translations for voider
From our Multilingual Translation Dictionary
- VoiderGerman
Get even more translations for voider »
Find a translation for the voider definition in other languages:
Select another language:
Discuss these voider definitions with the community:
Word of the Day
Would you like us to send you a FREE new word definition delivered to your inbox daily?
Use the citation below to add this definition to your bibliography:
"voider." Definitions.net. STANDS4 LLC, 2018. Web. 23 Mar. 2018. <https://www.definitions.net/definition/voider>.


text: H'lo! Regarding 'ABI Prism 377XL Collection' software version 2.6, I read with interest in http://www.appliedbiosystems.com/support/download/ga/377/ub/pdf/4313687.pdf the following: "Applescript=AE support This application now supports an Apple event that l= ets you import a text file. The information from the text file is used to fill out a sample sheet and, optionally, a run sheet based on the imported sampl= e sheet." However, I've not been able to make it work (yet) and my requests for support (GALAB at appliedbiosystems.com =3D The Genetic Analysis Technical Support Group, Applied Biosystems) come up dry Any one out there got it working? Willing to share their snippet of applescript with me? Thanks, Malcolm Cook (858) 623-7654 BioInformatics DNA Science Laboratories ---