Glycosylation of endogenous protein(s) of the rough and smooth microsomes by a lipid sugar intermediate.
Several problems regarding the protein acceptor of the oligosaccharide from GEA (glucosylated endogenous acceptor) were investigated in the present work using rat liver microsomal subfractions. It was found that the acceptor molecule is present in rough and smooth liver microsomes. Furthermore both fractions have closely similar specific activities. The problem of whether nascent peptides must be ribosome bound for glycosylation to occur was studied. The results suggests that binding of peptides to ribosomes is not a necessary condition for the transfer of GEA oligosaccharide to protein. The increase in specific activity found after partial release of the microsomal vesicular content suggests that the acceptor protein for GEA is membrane bound. Evidence obtained in attempting to elucidate whether nascent or completed chains are glycosylated favours the later possibility.
D000818:Animals; D003840:Deoxycholic Acid / Q000494:pharmacology; D006017:Glycolipids / Q000378:metabolism*; D006023:Glycoproteins / Q000096:biosynthesis*; D007700:Kinetics; D008297:Male; D008862:Microsomes, Liver / Q000187:drug effects / Q000378:metabolism*; D009844:Oligosaccharides / Q000378:metabolism; D011691:Puromycin / Q000494:pharmacology; D051381:Rats; D012270:Ribosomes / Q000378:metabolism
D006017:Glycolipids; D006023:Glycoproteins; D009844:Oligosaccharides; D003840:Deoxycholic Acid; D011691:Puromycin