title: Characterization of the oligosaccharide units of the fourth component of complement (Ss protein) synthesized by murine macrophages.
abstract: The glycosylation of murine C4 (Ss protein) synthesized by peritoneal macrophages has been investigated. Both the intracellular precursor, P-C4 (185), and the C4 alpha- and beta-chains that were secreted into medium were found to be glycosylated; however, no carbohydrate units were detected on the gamma-chain. Analyses of the oligosaccharide units showed that P-C4 (185) appears to contain both a "complex" and a "high mannose" carbohydrate group, the alpha-chain a "complex" group and the beta-chain a "high mannose" carbohydrate unit.
mesh_terms: D000118:Acetylglucosaminidase / Q000494:pharmacology; D000818:Animals; D001798:Blood Proteins / Q000096:biosynthesis*; D002850:Chromatography, Gel; D003181:Complement C4 / Q000096:biosynthesis* / Q000378:metabolism; D006020:Glycopeptides; D008264:Macrophages / Q000276:immunology*; D008358:Mannose; D051379:Mice; D008809:Mice, Inbred C3H; D009844:Oligosaccharides / Q000276:immunology*
chemical_list: D001798:Blood Proteins; D003181:Complement C4; D006020:Glycopeptides; D009844:Oligosaccharides; D000118:Acetylglucosaminidase; D008358:Mannose