Glycosyltransferases with endogenous acceptor activity in plasma membranes isolated from rat liver |
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Authors: | W.D. Merritt D.J. Morre W.W. Franke T.W. Keenan |
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Affiliation: | 1. Departments of Biological Sciences, Medicinal Chemistry and Pharmacognosy, and Animal Sciences, Purdue University, West Lafayette, Ind. 47907, U.S.A.;2. Division of Membrane Biology and Biochemistry, Institute of Experimental Pathology, German Cancer Research Center, 69 Heidelberg, G.F.R. |
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Abstract: | Plasma membrane fractions from rat liver exhibited glycosyltransferase activity with endogenous membrane-associated acceptors and either UDP-galactose, UDPglucose, UDP-N-acetylglucosamine, or GDPmannose donors. Of these, incorporation into non-lipid acceptors was most active with UDP-galactose and only with UDPgalactose and UDPmannose was there incorporation into endogenous lipid acceptors. CMP-N-acetylneuraminic acid was inactive as a donor with the isolated plasma membranes. In order to demonstrate transferase activity, low concentrations of substrate sugar nucleotides and short incubation times were used as well as sulfhydryl protectants and a phosphatase inhibitor (NaF) in the reaction mixtures. The findings support the concept of surface localization of at least a galactosyl transferase in cells of rat liver. |
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