Comparison of Acid Phosphatases in the Rat Prostatic Complex and Seminal Vesicles

Abstract

Acid phosphatase activity of different parts (ventral, lateral and posterior lobes and coagulating gland) of the rat prostatic complex and seminal vesicles were analyzed in homogenate and after fractionation with gel filtration and chromatofocusing. Significant differences between the various tissue homogenates were recorded in the hydrolysis of p-nitrophenyl phosphate, α-naphthyl phosphate and naphthol ASBI phosphate and the percentage of the tartrate-resistant activity varied from about 30 (in seminal vesicles) to 56 (in coagulating gland). Gel filtration resulted in the appearance of 2 (Sephadex G-200) to 3 (Sepharose 6B) activity peaks (GF-1 to GF-3). Studies with 6 substrates (p-nitrophenyl phosphate, α-naphthyl phosphate, β-naphthyl phosphate, naphthol ASBI phosphate, phenolphthalein phosphate and thymolphthalein phosphate) showed some relative differences in the hydrolysis rates as well as indications for possible overlapping of multiple enzymes in these peaks. Chromatofocusing of the ventral prostate homogenate resulted in the appearance of 8 activities (CF-1 to CF-8) with different pi-values (8.2, 8.1, 7.9, 7.1, 6.4, 6.0, 5.5 and 5.0), substrate preferences, pH-optima (5.5, 4.2, 4.2, 6.0, 5.5, 5.0, 4.2 and 5.0), molecular weights and modifier characteristics. The other tissues contained a lower number of these activities: 4 (CF-1 to CF-3 and CF-6) in lateral and posterior lobes and coagulating gland and 5 (CF-1 to CF-4 and CF-6) in seminal vesicles. The correspondence of the enzyme peaks after gel filtration and chromatofocusing was analyzed by refractionation. This indicated that some of the enzymes (GF-1, CF-5, CF-8) may appear in polymeric/aggregate forms. The differences in the acid phosphatase pattern suggest characteristic functional features in the various parts of the rat prostatic complex.