5α-Dihydrotestosterone Binding Protein in Rat Ventral Prostate; Purification, Nuclear Incorporation, and Subnuclear Localization

A yeast protein that binds nuclear localization signals: purification localization, and antibody inhibition of binding activity

Short stretches of amino acids, termed nuclear localization sequences (NLS), can mediate assembly of proteins into the nucleus. Proteins from the yeast, Saccharomyces cerevisiae, have been identified that specifically recognize nuclear localization peptides (Silver, P., I. Sadler, and M. A. Osborne. 1989. J. Cell Biol. 109:983-989). We now further define the role of one of these NLS-binding pro...

Direct evidence on incorporation of the receptor into the nuclei of rat ventral prostate in the form of the complex with dihydrotestosterone.

Cytosol 9S receptor was prepared from the supernatant fluid at 105,000 X g of rat prostate homogenates by a Sephadex G-100 gel chromatography, and was labeled with 131I. The 131I-labeled 9S receptor retained the activity of forming a complex with 3H-dihydrotestosterone, similarly to the intact cytosol receptor, when examined by a sucrose density gradient centrifugation. When the 131I-labeled cy...

PURIFICATION, PAHflAL CHARACTERIZATION OF RAT KIDNEY HYALURONIC ACID-BINDING PROTEIN AND ITS LOCALIZATION ON THE CELL

Immunochemical characterization of the androgen-dependent spermine-binding protein of the rat ventral prostate.

A solid-phase radioimmunoassay was developed to measure the level of the androgen-dependent spermine-binding protein (SBP) in the cytosol fraction of the rat ventral prostate during endocrine manipulation. The concentration of SBP and immunologically cross-reacting material (CRM) in the ventral prostate was at least 5000 times higher than the level of CRM detected in rat serum or cytosol from o...

Study of a proline-rich polypeptide bound to the prostatic binding protein of rat ventral prostate.

A proline-rich polypeptide is associated with prostatic binding protein, a major androgen-dependent protein described previously in the rat ventral prostate. This polypeptide has been purified. Its molecular weight estimated by gel filtration is about 8500, but a markedly lower value (3300) is obtained by sodium dodecyl sulfate-urea polyacrylamide gel electrophoresis. Isoelectric focusing on th...