Characterization of the oligosaccharide units of the fourth component of complement (Ss protein) synthesized by murine macrophages.
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.
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*
D001798:Blood Proteins; D003181:Complement C4; D006020:Glycopeptides; D009844:Oligosaccharides; D000118:Acetylglucosaminidase; D008358:Mannose