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- W338618371 abstract "Publisher Summary This chapter discusses glycolipid intermediates involved in the transfer of acetylglucosamine to the endogenous proteins found in yeast. In an earlier study, the isolation, from a particulate membrane fraction of yeast, of two glycolipids characterized as polyprenyl N-acetyl-glucosaminyl pyrophosphate (GlcNAc–P–P–Dol) and polyprenyl di-acetylchitobiosyl pyrophosphate was studied. The sugar moiety linked to protein is di-N-acetylchito-biose. This chapter describes a study to examine the initial glycosylation of acceptor proteins in the isolated plasmalemma. Yeast is grown in a chemostat. This preparation was partly contaminated with mitochondrial membranes. The formation of GlcNAc-lipids, GlcNAc incorporation into endogenous proteins, and characterization of carbohydrate attached to protein was studied. Incubation of the plasmalemma preparation with UDP–3H–GlcNAc resulted in the formation of labeled GlcNAc–P–P–Dol and (GlcNAc) 2-P-P-Do1 in the ratio 3:2, and of 3H–GlcNAc incorporation into endogenous proteins. These results suggest that besides the transfer of GlcNAc residues via lipid-intermediates, a direct transfer of GlcNAc from UDP–GlcNAc to acceptor proteins can take place." @default.
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- W338618371 date "1979-01-01" @default.
- W338618371 modified "2023-09-27" @default.
- W338618371 title "Glycolipid Intermediates Involved in the Transfer of N-Acetylglucosamine to Endogenous Proteins in Yeast" @default.
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- W338618371 doi "https://doi.org/10.1016/b978-0-12-301302-6.50035-x" @default.
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