作者: W. HEYNS , P. MOOR
DOI: 10.1111/J.1432-1033.1977.TB11733.X
关键词: Sephadex 、 Biochemistry 、 Cytosol 、 Serum albumin 、 Chemistry 、 Prostatein 、 Chromatography 、 Binding site 、 Polyacrylamide gel electrophoresis 、 Binding protein 、 Pregnenolone
摘要: Rat prostatic cytosol contains a high concentration of binding protein with peculiar steroid-binding properties. Indeed, in spite relatively low affinity, charcoal adsorption can be used for its measurement. Furthermore, the is not specific particular steroids and increases very strongly after delipidation. In delipidated site 3.1 μ mol/g apparent affinity pregnenolone 1.7 × 106 M−1. The fluid shows that this substance secreted by prostate. Prostatic has following physicochemical characteristics: it precipitated ammonium sulfate between 50 70% saturation; elution position from Sephadex G-100 column corresponds to molecular weight 51000; sediments sucrose density gradients at 3.7 S eluted DEAE-cellulose columns about 0.25 M KCl. On polyacrylamide gel electrophoresis activity coincides major cytosolic band. This band same mobility as serum albumin 7% gels, but higher more concentrated gels.