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 homologs identical with those isolated directly from S. cerevisiae (baker''s yeast). No particular homolog was preferred in the enzymic transfer of N-acetylglucosamine 1-phosphate to endogenous dolichol monophosphate.