Cellular retinoic acid-binding protein from rat testis. Purification and characterization.
Cellular retinoic acid-binding protein has been purified to homogeneity from rat testes. The procedures utilized in the purification included acid precipitation, gel filtration, and chromatography on DEAE-cellulose. The binding protein was purified approximately 12,000-fold, based on total soluble testicular protein. The protein is a single polypeptide chain with a molecular weight of 14,600, determined by information from gel filtration and sodium dodecyl sulfate-polyacrylamide electrophoresis. The protein binds retinoic acid with high affinity; the apparent dissociation constant was determined by fluorometric titration to be 4.2 X 10(-9) M.
D000818:Animals; D002352:Carrier Proteins / Q000302:isolation & purification* / Q000378:metabolism; D008297:Male; D008722:Methods; D008970:Molecular Weight; D051381:Rats; D012177:Retinol-Binding Proteins / Q000378:metabolism; D013057:Spectrum Analysis; D013737:Testis / Q000032:analysis*; D014212:Tretinoin / Q000378:metabolism*; D014801:Vitamin A / Q000031:analogs & derivatives*
D002352:Carrier Proteins; D012177:Retinol-Binding Proteins; D014801:Vitamin A; D014212:Tretinoin