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 ammonium sulfate, 10 mm Tris, pH 8.0. The crystals are space group P2(1), with a = 39.4, b = 58.9, c = 65.4 a, beta = 105 degrees 16 min.
Newcomer
M E
ME
Department of Biochemistry, Vanderbilt University, Nashville, Tennessee 37232.
Ong
D E
DE
D000595:Amino Acid Sequence; D000818:Animals; D002352:Carrier Proteins / Q000302:isolation & purification* / Q000378:metabolism; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D003460:Crystallization; D004822:Epididymis / Q000378:metabolism*; D008297:Male; D008969:Molecular Sequence Data; D011487:Protein Conformation; D051381:Rats; D018168:Receptors, Retinoic Acid; D013056:Spectrophotometry, Ultraviolet; D014212:Tretinoin / Q000378:metabolism; D014961:X-Ray Diffraction
D002352:Carrier Proteins; D018168:Receptors, Retinoic Acid; D014212:Tretinoin