Prostate alpha-protein. Isolation and characterization of the polypeptide components and cholesterol binding.

alpha-Protein, a major glycoprotein in the cytosol fraction of rat ventral prostate, has a molecular weight of about 50,000 and can be dissociated, by sodium dodecyl sulfate, into two different subunits (A and B). alpha-Protein has three different polypeptide components with apparent molecular weights of 10,000 (I), 14,000 (II), and 15,000 (III). These components were purified to homogeneity and their amino acid compositions were determined. Subunit A is composed of Components I and III, whereas subunit B is composed of Components II and III. Carbohydrate was detectable only on Component III. Component III isolated from subunit A and Component III isolated from subunit B appear to be identical. The purified alpha-protein contains 0.7-1 mol of cholesterol/mol of protein. If cholesterol was removed by acetone, about 1 mol of 5 alpha-dihydrotestosterone or pregnenolone could bind to 1 mol of alpha-protein. In the presence of 2 mM ZnCl2, alpha-protein can form dimers and tetramers. In cell-free systems, alpha-protein can inhibit binding of the androgen-receptor complex to nuclear chromatin and also can promote the release of the complex already bound to chromatin. This effect is due to polypeptide Component I.