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ANTI GLYCATION EFFECT OF WHITTON ROOT (EULOPHIA NUDA) IN-VITRO CONDITION IN RELATION TO DIABETES MELLITUS

Non enzymatic glycation takes place when elevated levels of reduced sugars react with amino groups of proteins and is called as advanced glycation end products (AGEs) are responsible for Diabetes Mellitus. Hydroalcoholic extract of Whitton root (Eulophia nuda) was tested for in-vitro inhibition of nonenzymatic glycation of Immunoglobin G. Plant extracts have their own importance and now being studied extensively due to having little or no side effects in all aspects of life sciences from botany to medicine in biochemical research. In present study Whitton root was selected and used to check the glycation inhibitory activity in-vitro condition. Various combinations of glucose, protein and Whitton root extracts were made under in vitro conditions and their activity was monitored with Trichloro acetic acid treatment method at 350 nm. Glycated products/ AGEs were more with high glucose and high protein concentration and these were decreased by highest concentration of Whitton root extract i.e. 30 mg/mL or 300 μL. Lower concentrations of plant extract produced either no or least response against advanced glycation end products (AGEs). INTRODUCTION: Nonenzymatic glycation of protein by reducing sugars is a complicated pathway of various modifications that lead to formation of advanced glycation end products (AGEs). Stable Amadori products are formed by organic reactions with the Schiff base which will further undergo a series of reactions through dicarbonyl intermediates to form AGEs. It is also assumed to be formed by sequential glycation and oxidation reactions called glycoxidation. The accumulation of the reaction products of protein glycation in living organisms leads to structural and functional modifications of tissue proteins . The role of Advanced glycated end-product proved to be significantly responsible in diabetic microvascular complications of retinopathy, neuropathy and nephropathy as well as their role in the accelerated hyperlipidemia . There is evidence that glycosylation leads to biochemical modification of Immunoglobulin, and other macromolecules and is cause for pathogenesis of diabetic complications . Elevated glucose level is etiologic agent for the pathogenesis of diabetic complications by increasing protein glycation and formation of advanced glycation end products (AGEs).