Glycosyl transfer from nucleotide sugars to C85- and C55-polyprenyl and retinyl phosphates by microsomal subfractions and Golgi membranes of rat liver.
The capacity of isolated membrane fractions to catalyse transfer of sugars from sugar nucleotides to alpha-saturated and non-saturated forms of phosphorylated C85 and C55 polyprenols and retinyl phosphate was examined. The amount of endogenous lipid acceptor present for various sugars was also measured. It appears that the types and amounts of polyprenyl phosphates present in rough- and smooth-microsomal fractions and Golgi membranes are different and the individual polyprenyl phosphates exhibit specificity as sugar acceptors.
D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D004224:Diterpenes; D006056:Golgi Apparatus / Q000378:metabolism*; D066298:In Vitro Techniques; D008099:Liver / Q000378:metabolism; D008297:Male; D008563:Membrane Lipids / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism; D008862:Microsomes, Liver / Q000378:metabolism*; D009702:Nucleoside Diphosphate Sugars / Q000378:metabolism*; D011106:Polyisoprenyl Phosphates / Q000378:metabolism*; D051381:Rats; D014801:Vitamin A / Q000031:analogs & derivatives / Q000378:metabolism
D004224:Diterpenes; D008563:Membrane Lipids; D008565:Membrane Proteins; D009702:Nucleoside Diphosphate Sugars; D011106:Polyisoprenyl Phosphates; D014801:Vitamin A; C012532:retinol phosphate