The asparagine-linked carbohydrate of honeybee venom hyaluronidase

Publisher Website
Google Scholar
Abstract
Hyaluronidase from the venom of the honeybee (Apis mellifera) has been purified by gelpermeation and cation exchange chromatography. Its asparagine-linked carbohydrate chains were released from tryptic glycopeptides with N-glycosidase A and reductively aminated with 2-aminopyridine. Separation of the fluorescent derivatives by size-fractionation and reversed-phase HPLC afforded eighteen fractions which were analysed by two-dimensional HPLC mapping combined with exoglycosidase digestions. The bulk of the N-linked glycans of hyaluronidase consisted of small oligosaccharides (Man1–3GlcNAc2), most of which were either α1,3-monofucosylated or α1,3-(α1,6-)difucosylated at the innermost GlcNAc residue. High-mannose type structures constituted the minor fractions, together making up about 5% of the oligosaccharide pool from hyaluronidase. Four fractions, making up 8% of the N-linked glycans, contained the terminal trisaccharide GalNAcβ1-4[Fucα1-3]GlcNAcβ1- in β1,2-linkage to the core α1,3-mannosyl residue. No evidence for the presence of O-glycans or sialic acids could be found.

This publication has 19 references indexed in Scilit: