The polyenic system of retinyl phosphate is required for its mannosyl donor activity but not for acceptor activity.

Y. Shidoji, C. S. Silverman-Jones, L. M. De Luca

Research output: Contribution to journalArticlepeer-review

Abstract

We investigated whether the polyenic and allylic phosphate systems of retinyl phosphate are essential for its mannosyl acceptor and donor activities in rat liver postnuclear membranes. Perhydromonoeneretinyl phosphate, a compound without growth-promoting activity in vitamin A-deficient animals, was prepared by catalytic hydrogenation of retinol and phosphorylation. Perhydromonoeneretinyl phosphate mannose synthesis from GDP-mannose showed continued accumulation for at least 60 min, while retinyl phosphate mannose synthesis showed a maximum at 20-30 min and then declined. Moreover, only retinyl phosphate stimulated transfer of mannose from GDP-mannose to endogenous proteins, which were separated by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. Thus, hydrogenation of side-chain double bonds in retinyl phosphate impaired only slightly its mannosyl acceptor activity, but caused loss of mannosyl donor activity.

Original languageEnglish (US)
Pages (from-to)865-868
Number of pages4
JournalThe Biochemical journal
Volume208
Issue number3
DOIs
StatePublished - Dec 15 1982
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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