Glycans of synaptosomal plasma membrane glycoproteins from adult rat forebrain: Characterization after fractionation by concanavalin A-Sepharose affinity chromatography

摘要: Abstract Glycopeptides obtained by exhaustive proteolytic digestion of synaptosomal plasma membranes from adult rat forebraini were separated affinity chromatography on concanavalin A-Sepharoe. Concanavalin A-binding glycopeptides are essentially made up mannose and N-acetylglucosamine in a molar ration 3.45:1, whereas not bound to A have complex monosaccharide composition. By gel filtration Bio-Gel P-30, appear as low-molecular-weight (migrating like ovalbumin glycopeptides), behave high-molecular-weight fetuin glycopeptides). Comparison brain with glycoproteins isolated the same membrane fraction shows clear differences monosccharide We demonstrate here that this discrepancy is due presence most glycoprotein subunits at least two different types glycan: addition glycans, these carry other glycans which do interact A. Biological implications (or more) glycan polypeptide discussed.