Glycoprotein synthesis in gastric epithelial cells of the rat. Properties of microsomal glycoprotein glycosyltransferases.
1. Optimal assay conditions were determined for a microsomal glycoprotein galactosyl- and fucosyltransferase derived from gastric epithelial scrapings with both exogenous and endogenous acceptor glycoprotein. 2. Subcellular fractionation of the homogenate yielded microsomal fractions enriched in glycosyltransferases. 3. The effect of feeding on galactosyltransferase activity per cell was examined. 4. Endogenous acceptor molecules were identified as glycoproteins after labeling by means of UDP-[3H]galactose in the cell-free system.
D000818:Animals; D004847:Epithelial Cells; D004848:Epithelium / Q000201:enzymology; D005643:Fucose; D005700:Galactosyltransferases / Q000378:metabolism*; D005753:Gastric Mucosa / Q000201:enzymology*; D006023:Glycoproteins / Q000096:biosynthesis*; D007700:Kinetics; D008297:Male; D008345:Manganese / Q000494:pharmacology; D008861:Microsomes / Q000201:enzymology*; D011092:Polyethylene Glycols / Q000494:pharmacology; D051381:Rats; D013347:Subcellular Fractions / Q000201:enzymology; D014166:Transferases / Q000378:metabolism*
D006023:Glycoproteins; D005643:Fucose; D011092:Polyethylene Glycols; D008345:Manganese; D014166:Transferases; D005700:Galactosyltransferases