Lipid-mediated glycosylation of endogenous proteins in isolated plasma membrane of Saccharomyces cerevisiae.
A highly purified plasma membrane fraction from Saccharomyces cerevisiae was obtained by centrifugation on discontinuous sucrose and Urografin gradients. This plasma membrane fraction was capable of glycosylating endogenous proteins. It is shown that glycolipids play an intermediate role in these glycosylation reactions; with uridine 5'-diphosphate-N-acetylglucosamine as sugar donor the intermediate lipids possessed stability towards alkali and chromatographic mobilities similar to polyprenyl diphosphate N-acetylglucosamine and polyprenyl diphosphate di-N-acetylchitobiose.
D002458:Cell Fractionation; D002462:Cell Membrane / Q000378:metabolism; D005656:Fungal Proteins / Q000378:metabolism*; D006017:Glycolipids / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000378:metabolism / Q000648:ultrastructure*; D014537:Uridine Diphosphate N-Acetylglucosamine / Q000378:metabolism
D005656:Fungal Proteins; D006017:Glycolipids; D008565:Membrane Proteins; D014537:Uridine Diphosphate N-Acetylglucosamine