Isolation and characterization of binding proteins for retinol from the cytosol, nucleosol and chromatin of the oviduct magnum of laying hens.
Protein fractions that bind retinol were isolated from the cytosol, nucleosol and chromatin of the oviduct magnum of laying hens. The proteins isolated from the three sources showed similar elution profiles on chromatography through Sephadex G-75 and G-50 columns, and comparable mobility during electrophoresis on sodium dodecyl sulphate/polyacrylamide gels. Their molecular weights were calculated to be around 14500. When oviducts from vitamin A-depleted and vitamin A-repleted immature chicks given oestrogen injections for 6 consecutive days were incubated with [3H]retinyl acetate, uptake of the radioactivity in the nuclei of the vitamin A-depleted tissue was severalfold higher than that in the nuclei from the vitamin A-repleted tissue.
D000818:Animals; D002467:Cell Nucleus / Q000032:analysis; D002645:Chickens; D002843:Chromatin / Q000032:analysis; D002850:Chromatography, Gel; D003600:Cytosol / Q000032:analysis; D004967:Estrogens / Q000494:pharmacology; D066298:In Vitro Techniques; D010057:Oviducts / Q000032:analysis* / Q000187:drug effects; D012177:Retinol-Binding Proteins / Q000302:isolation & purification*; D014801:Vitamin A / Q000378:metabolism; D014802:Vitamin A Deficiency / Q000378:metabolism
D002843:Chromatin; D004967:Estrogens; D012177:Retinol-Binding Proteins; D014801:Vitamin A