Sani B P, Banerjee C K
Biochem J. 1978 Aug 1;173(2):643-9. doi: 10.1042/bj1730643.
Retinoic acid-binding protein, which is considered to mediate the biological function of retinoic acid in epithelial differentiation and in the possible control of tumorigenesis, was reproducibly purified from chick-embryo skin by using DEAE-Sephadex and Sephadex G-100 column chromatography and isoelectric focusing. About 1mg of protein was isolated from 60g of skin. The purified protein-ligand complex was found to be homogeneous by electrophoresis on polyacrylamide gels. The binding protein has mol.wt. 17800 and pI 4.5. The binding of [3H]retinoic acid to the protein was completely inhibited by mercury compounds. The inhibition is reversible on treatment without dithithreitol; about 50% of the retinoic acid-binding capacity of the mercury-compound-treated protein is restored by chromatography on Sephadex G-25. iodoacetamide treatment of the protein irreversibly inhibits about 50% of retinoic acid binding.
视黄酸结合蛋白被认为可介导视黄酸在上皮分化以及可能的肿瘤发生控制中的生物学功能。通过使用二乙氨基乙基葡聚糖（DEAE - Sephadex）和葡聚糖凝胶G - 100柱色谱法以及等电聚焦，可从鸡胚皮肤中反复纯化得到该蛋白。从60克皮肤中分离出了约1毫克蛋白质。通过聚丙烯酰胺凝胶电泳发现纯化的蛋白质 - 配体复合物是均一的。该结合蛋白的分子量为17800，等电点为4.5。汞化合物可完全抑制[3H]视黄酸与该蛋白的结合。在没有二硫苏糖醇的处理下，这种抑制是可逆的；经葡聚糖凝胶G - 25柱色谱法处理后，汞化合物处理过的蛋白的视黄酸结合能力约恢复50%。用碘乙酰胺处理该蛋白会不可逆地抑制约50%的视黄酸结合。
