Control of glycoprotein synthesis. The purification by preparative high voltage paper electrophoresis in borate of glycopeptides containing high mannose and complex oligosaccharide chains linked to asparagine.
The heterogeneity of glycopeptides prepared from pronase digests of various glycoproteins has previously been demonstrated primarily by lengthy paper chromatography of oligosaccharides released from the glycopeptides by enzymatic or chemical means. We describe the use of high voltage paper electrophoresis in borate for the resolution of seven glycopeptides from ovalbumin and seven glycopeptides from human immunoglobulin G. This technique has been used in the preparation of glycopeptide substrates required for the study of certain glycosyltransferases and glycosidases.
D001216:Asparagine / Q000032:analysis; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D006020:Glycopeptides / Q000302:isolation & purification*; D006023:Glycoproteins / Q000096:biosynthesis; D006801:Humans; D007074:Immunoglobulin G; D008358:Mannose / Q000032:analysis; D009844:Oligosaccharides / Q000302:isolation & purification*; D010047:Ovalbumin; D011485:Protein Binding
D006020:Glycopeptides; D006023:Glycoproteins; D007074:Immunoglobulin G; D009844:Oligosaccharides; D001216:Asparagine; D010047:Ovalbumin; D008358:Mannose