THE INVESTIGATION OF GLYCOSAMINOGLYCAN MIMOTOPE STRUCTURE USING CAPILLARY ELECTROPHORESIS AND OTHER COMPLEMENTARY ELECTROPHORETIC TECHNIQUES

We have used various electrophoretic techniques to analyse glycosamino glycan structure. Capillary electrophoresis has been particularly usef ul in the determination of the sulphation of glycosaminoglycans (GAG) and the sulphation of partly desulphated glycosaminoglycans produced b y methanolysis. This, in conjunction with preparative electrophoresis and enzyme linked immunosorbent assay (ELISA) has permitted us to asce rtain the length of the oligosaccharide required for binding and sulph ate ester groups required for optimal binding and those essential for antibody binding. From these preliminary studies, we have demonstrated that the minimum length of oligosaccharide required for binding was a bout 12-14 monosaccharides in length. It appears likely that 6 sulphat ion is required for strong binding but 4 sulphation is not involved in mimotope binding. We propose on the basis of this evidence that the m imotope does not contain 4- sulphate residues but 3-4 6-sulphate ester groups are essential for binding.