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The investigation of glycosaminoglycan mimotope structure using capillary electrophoresis and other complementary electrophoretic techniques
Author(s) -
Carney Stephen L.,
Caterson Bruce,
Penticost Helen R.
Publication year - 1996
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150170216
Subject(s) - sulfation , capillary electrophoresis , mimotope , glycosaminoglycan , chemistry , electrophoresis , oligosaccharide , monosaccharide , chromatography , biochemistry , peptide , phage display
We have used various electrophoretic techniques to analyse glycosaminoglycan structure. Capillary electrophoresis has been particularly useful in the determination of the sulphation of glycosaminoglycans (GAG) and the sulphation of partly desulphated glycosaminoglycans produced by methanolysis. This, in conjuction with preparative electrophoresis and enzyme linked immunosorbent assay (ELISA) has permitted us to ascertain the length of the oligosaccharide required for binding and sulphate 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 about 12–14 monosaccharides in length. It appears likely that 6 sulphation is required for strong binding but 4 sulphation is not involved in mimotope binding. We propose on the basis of this evidence that the mimotope does not contain 4‐sulphate residues but 3‐4 6‐sulphate ester groups are essential for binding.