Purification and crystallization of a retinoic acid-binding protein from rat epididymis. Identity with the major androgen-dependent epididymal proteins
The retinoic acid binding activity in the lumen of the rat epididymis (Ong, D., and Chytil, F. (1988) Arch. Biochem. Biophys. 267, 474-478) has been purified to homogeneity. The protein exists in two forms, one form having an additional three amino acids at the amino terminus. The amino acid sequence of the protein was determined to 20 amino acids and proved to be identical to that of the major androgen-dependent proteins from rat epididymis as deduced from the cDNA sequence. These proteins are thought to play a role in sperm maturation, perhaps, it can be suggested now, by delivering retinoic acid to the sperm. The retinoic acid-binding protein has sequence homology to the serum retinol-binding protein and is predicted to have the same overall fold of the polypeptide chain. The epididymal retinoic acid-binding protein has been crystallized from 39 to 43% saturated ammonion sulfate, 10 mm Tris, pH 8.0. The crystals are space group P21, which a = 39.4, b = 58.9, c = 65.4 a, β = 105° 16 min.
Publication Source (Journal or Book title)
Journal of Biological Chemistry
Newcomer, M., & Ong, D. (1990). Purification and crystallization of a retinoic acid-binding protein from rat epididymis. Identity with the major androgen-dependent epididymal proteins. Journal of Biological Chemistry, 265 (22), 12876-12879. Retrieved from https://digitalcommons.lsu.edu/biosci_pubs/2750