Separable binding proteins for retinoic acid and retinol in bovine retina.
Binding proteins for retinoic acid and retinol were separated from a supernatant prepared from bovine retina. Fraction IV from DEAE-cellulose chromatography bound exogenous [3H] retinoic acid which could not be effectively displaced by retinol, retinal, retinyl acetate or palmitate, but which was readily displaced with excess retinoic acid. [3H] Retinol was bound by fraction V from DEAE-cellulose chromatography and was not displaced by retinal, retinoic acid, retinyl acetate or retinyl palmitate, but was readily displaced by excess retinol. Unlike bovine serum retinol-binding protein, neither intracellular binding protein formed a complex with purified human serum prealbumin. The supernatant from bovine retinas was estimated to contain five times more retinoic acid binding than retinol binder.
D000818:Animals; D002417:Cattle; D011485:Protein Binding; D011506:Proteins / Q000302:isolation & purification* / Q000378:metabolism; D012160:Retina / Q000378:metabolism*; D012177:Retinol-Binding Proteins / Q000302:isolation & purification* / Q000378:metabolism; D014212:Tretinoin / Q000378:metabolism*; D014801:Vitamin A / Q000031:analogs & derivatives* / Q000378:metabolism*
D011506:Proteins; D012177:Retinol-Binding Proteins; D014801:Vitamin A; D014212:Tretinoin