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 language | English (US) |
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Pages (from-to) | 865-868 |
Number of pages | 4 |
Journal | The Biochemical journal |
Volume | 208 |
Issue number | 3 |
DOIs | |
State | Published - Dec 15 1982 |
Externally published | Yes |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology