Studies on human prostatic acid phosphatase. V. Isolation and characterization of a prostatic acid phosphatase isozyme.

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Abstract
Acid phosphatase isozyme 4 (pI [isoelectric point] 6.1) was isolated from human prostate tissue. The enzyme showed a single protein band when examined by polyacrylamide gel disc electrophoresis. The purification coefficient was .apprx. 3.2 and the recovery of enzyme activity was 0.1% from the supernatant fraction. The MW of the enzyme obtained by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate was 79,000. The enzyme was not cross-reactive with acid phosphatase isozyme (pI 5.3) in immunodiffusion. Isozyme 4 had almost the same enzymic properties (Km, Ki and optimum pH) as isozyme 2, but the specific activity of isozyme 4 was 1/4 of that of the latter.