Human Prostatic Acid Phosphatases: I. Isolation

A new purification procedure is described for the human prostatic acid phosphatase. The procedure included carboxy-methyl-Sephadex and Concanavalin A affinity column chromatography. The purified enzyme has a high specific enzyme activity and is free from any extraneous proteins judging from immunochemical criteria and biochemical criteria such as SDS-polyacrylamide gel electrophoresis. The purified enyzme produced a monospecific anti-PAP antisera in animals and this anti-PAP antibody did not cross-react with other human acid phosphatases.