Characterization of MOPC 315 IgA oligosaccharide processing intermediates.
The structures of alpha 1,2-mannose containing partially processed asparagine-linked oligosaccharides on the alpha-chain of MOPC 315 IgA were characterized using specific glycosidases and acetolysis. Man6GlcNAc2, a substrate for a Golgi alpha 1,2-mannosidase, was found to be a single isomeric structure. Likewise, Man7-9GlcNAc2 were single isomers indicating an ordered sequence of removal of alpha 1,2-linked mannose residues on this murine immunoglobulin heavy chain.
D000118:Acetylglucosaminidase; D000818:Animals; D002240:Carbohydrate Sequence; D002851:Chromatography, High Pressure Liquid; D007070:Immunoglobulin A / Q000378:metabolism*; D007143:Immunoglobulin Heavy Chains / Q000378:metabolism; D007536:Isomerism; D008358:Mannose / Q000378:metabolism; D008361:Mannosidases / Q000378:metabolism; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase; D051379:Mice; D009844:Oligosaccharides / Q000378:metabolism*; D010954:Plasmacytoma / Q000276:immunology*; D043323:alpha-Mannosidase
D007070:Immunoglobulin A; D007143:Immunoglobulin Heavy Chains; D009844:Oligosaccharides; D008361:Mannosidases; D043323:alpha-Mannosidase; D000118:Acetylglucosaminidase; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase; D008358:Mannose