Studies on Human Prostatic Acid Phosphatase. I. Effect of Detergent and Bovine Serum Albumin on Hydrolysis of Various Substrates by Purified Prostatic Acid Phosphatase

Abstract

Prostatic acid phosphatase was purified from human prostate gland by ammonium sulfate fractionation, phosphate-cellulose, Sephadex G-100, and DEAE-cellulose column chromatography. The purified enzyme was free of human serum protein and had a single protein corresponding to phosphatase activity by disc electrophoresis. Effect of various detergents and bovine serum albumin on hydrolysis of six substrates by purified prostatic acid phosphatase was investigated. Enhancing effect of various nonionic detergents and bovine serum albumin on hydrolysis of thymolphthalein monophosphate was observed. Optimal concentration of the enhancing effect was observed. In less than the optimal concentration, Lineweaver-Burk plots presented increase of K_m and V_max values, while in more than the optimal concentration K_m value increased without change in V_max value.