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- W1966342254 abstract "It is generally accepted that the biosynthesis of polysaccharide proteins in mammalian tissues follows a certain schedule [ 1,2] involving four principal steps: (a) formation of the polypeptide backbone, (b) stepwise addition of monosaccharide units from the appropiate nucleotide sugars to form the linkage j e ion to protein, and (c) the alternate addition of hex amine and uranic acid moieties from their respective UDP-sugars to the non-reducing terminus of the growing chain. Finally, (d) sulfation is accomplished by adding sulfate groups from 3’.phosphoadenosine-5’.phosphosulfate to certain of the monosaccharide moieties. The various glycosyltransferases involved are specific for the sugar residue to be transferred, as well as for the acceptor group. For example, transfer of N-acetylgalactosamine from UDPGalNAc to oligosaccharides with glucuronic acid in the non-reducing terminus was catalyzed by a particulate enzyme preparation from embryonic chick cartilage [3]. However the same preparation failed to catalyze the transfer of N-acetylgalactosamine to an oligosaccharide with iduronic acid as the terminal sugar [4] . The formation of an N-acetylgalactosaminidic linkage to an L-iduronosyl residue constitutes a" @default.
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- W1966342254 date "1971-08-01" @default.
- W1966342254 modified "2023-10-17" @default.
- W1966342254 title "Studies on the biosynthesis of dermatan sulfate" @default.
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- W1966342254 doi "https://doi.org/10.1016/0014-5793(71)80344-7" @default.
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