EVIDENCE FOR CELL-SURFACE GLYCOSYLTRANSFERASES
نویسندگان
چکیده
منابع مشابه
Evidence for Cell-surface Glycosyltransferases
Intact chicken embryo neural retina cells have been shown to catalyze the transfer of galactose-(14)C from uridine diphosphate galactose (UDP-galactose) to endogenous acceptors of high molecular weight as well as to exogenous acceptors. Four lines of evidence indicate that the galactosyltransferases catalyzing these reactions are at least partly located on the outside surface of the plasma memb...
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The biosynthesis and degradation of glycoconjugates are catalyzed by glycosyltransferases and glycosidases, respectively, and the genes which encode glycosyltransferases and related proteins are referred to as `glyco-genes'. The expression of glycosyltransferases, the substrate speci®city of the enzymes and their subcellular localization represent key determinants in the biosynthesis of sugar c...
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Normal and transformed mouse fibroblasts catalyze transfer of sialic acid, galactose, IV-acetylgalactosamine, N-acetylglucosamine, glucose, and mannose from nucleotide sugar donors to glycolipids and glycoproteins. The enzyme activity is associated with intact cells. Kinetic parameters and optimal ion concentrations have been determined for the glycosyltransferase activities detected when whole...
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Cell-surface galactosyltransferase was studied in suspensions of intact baby hamster kidney fibroblasts with both endogenous and exogenous glycoprotein acceptors. The cell-surface location of galactosyltransferase was demonstrated in experiments with the enzyme modifier alpha-lactalbumin, which does not enter the cell. The addition of alpha-lactalbumin to the assay medium for galactosyltransfer...
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Glycosyltransferases involved in the biosynthesis of glyco-protein and glycolipid sugar chains are resident membrane proteins of the endoplasmic reticulum and the Golgi apparatus. Although the glycosylation pathways in which they participate have been extensively studied and reviewed (1-3), major questions remain concerning the molecular basis for the subcellular organization of the glycosylati...
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ژورنال
عنوان ژورنال: Journal of Cell Biology
سال: 1971
ISSN: 1540-8140,0021-9525
DOI: 10.1083/jcb.51.2.536