| Literature DB >> 348196 |
F Reuvers, P Boer, F W Hemming.
Abstract
The lipid moiety of a lipid diphosphate N-acetylglucosamine, an intermediate in glycosylation of proteins, was studied. Ozonolysis of the compound gave evidence for an alpha-saturated isoprene unit. Alkaline hydrolysis of the glycolipid, followed by high-pressure liquid chromatography, showed the presence of a series of polyprenol homologues identical with those isolated directly from Saccharomyces cerevisiae (baker's yeast). No particular homologue was preferred in the enzymic transfer of N-acetylglucosamine 1-phosphate to endogenous dolichol monophosphate.Entities:
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Year: 1978 PMID: 348196 PMCID: PMC1183823 DOI: 10.1042/bj1690505
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857