前立腺の解燐酵素に関する研究 (1)ヒト前立腺フォスフォモノエステラーゼの精製とその免疫学的所見

Abstract

Prostatic phosphomonoesterase (prostatic PMEase) was purified by London's and Ostrowski's methods as follows. The first step is fullers' earth adsorption, the second step is fractionation with ammonium sulfate, the third step is DEAE cellulose column chromatography and the fourth step is rechromatography of a fraction obtained by the third step. The purified prostatic PMEase was in homogeneous form electrophoretically and ultracentrifugally. Four distinct peaks of protein were obtained by the DEAE cellulose column chromatography and the PMEase activity was exhibited in the three peaks except the first peak. Each peak of the purified materials by the DEAE cellulose column chromatography was examined by immunoelectrophoresis with antihuman prostatic PMEase serum of the rabbit. The PMEase of peak II migrates to the cathode, that of peak III migrates slightly to the anode and that of peak IV migrates to the anode more than that of peak III. It was found by immunoelectrophoresis that the prostatic PMEase which was in homogeneous form electrophoretically and ultracentrifugally, contained always siderophilin. Each PMEase fraction of the three peaks was examined on t h e enzymatic properties such as optimal pH., Michael's constant and inhibition test. The enzymatic properties of each PMEase fraction were slightly different each other.