Characterization of Lectin-Binding Glycolipids
{'Code': '08070400', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'MCB', 'LongName': 'Div Of Molecular and Cellular Bioscience'}}
{'SignBlockName': 'Eve Ida Barak', 'PO_EMAI': None, 'PO_PHON': None}
Lectin affinity chromatography has proven to be a powerful                      method to separate oligosaccharides based on their                              stereochemical structure.  Since glycolipids form micelles in                   aqueous solutions, studying their interactions with lectins is                  not amenable to methods used to study water soluble                             glycopeptides has been developed.  In addition to an                            immunoautoradiographic method to detect lectin-binding                          glycolipids on thin layer chromatograms.  A lectin affinity                     chromatographic method for the purification of intact                           glycolipids has been developed.  This method is based on the                    ability of Helix pomatia lectin colums to bind its                              oligosaccharide ligands in aqueous solutions of                                 tetrahydrafuran, which inhibit glycolipid miccelle formation                    and permit the separation of nonspecifically bound glycolipids.                 The general application of this method to other lectins will                    provide a novel approach to the purification of glycolipids.                    The ability to purify human blood group A-active glycolipds                     from a total lipid extract in a single chromatographic step on                  a column of Helix pomatia lectin will be exploited to                           structurally characterize metabolically labeled blood group A                   active glycolipids and glycopeptides form a huam epidermoid                     cell line A-431.  This metabolically active cell line will                      provide an excellent system to investigate the biosynthetic                     pathway of an oligosaccharide antigen synthesized by a single                   group of glycosyltransferases acting on different                               glyoconjugate precursors.                                                                                                                                       Lectins are proteins which have a specific affinity for certain                 carbohydrates.  The lectins can be attached to inert supports                   and placed in glass columns which can then be used to separate                  substances on the basis of their affinity for the lectins.                      This technique has been very useful in the separation of glyko                  proteins and carbohydrates, but not for lipids (fatty                           substances)  because the latter are not soluble in water.  The                  P.I. has now developed a method for using these columns in                      organic solvents in which the lipids are soluble.  This                         technique is of great promise in furthering our understanding                   of the metabolism of these lipids and how they function in cell                 membranes.
{'FirstName': 'David', 'LastName': 'Smith', 'PI_MID_INIT': 'F', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'David F Smith', 'EmailAddress': None, 'NSF_ID': '000369653', 'StartDate': '08/01/1988', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'Virginia Polytechnic Institute and State University', 'CityName': 'BLACKSBURG', 'ZipCode': '240603359', 'PhoneNumber': '5402315281', 'StreetAddress': '300 TURNER ST NW', 'StreetAddress2': 'STE 4200', 'CountryName': 'United States', 'StateName': 'Virginia', 'StateCode': 'VA', 'CONGRESSDISTRICT': '09', 'CONGRESS_DISTRICT_ORG': 'VA09', 'ORG_UEI_NUM': 'QDE5UHE5XD16', 'ORG_LGL_BUS_NAME': 'VIRGINIA POLYTECHNIC INSTITUTE & STATE UNIVERSITY', 'ORG_PRNT_UEI_NUM': 'M515A1DKXAN8'}
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{'Code': '1144', 'Text': 'Molecular Biophysics'}
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