Abstract
Prostatic acid phosphatase (PAP) was purified from human seminal plasma by precipitation with ammonium sulfate and by serial chromatographies with concanavalin A-Sepharose, Sephadex G-100, and carboxymethyl-cellulose. The purified enzyme was found to be homogeneous by polyacrylamide gel electrophoresis, both with and without sodium dodecyl sulfate. The purified enzyme also gave a single precipitin line upon immunoelectrophoresis, when reacted with rabbit antiserum to seminal plasma. A simple method was developed for the preparation of monospecific antibody to PAP. In addition, a new immunoenzymatic assay system for PAP is reported, utilizing filter paper discs as a solid-phase to which monospecific antibody to PAP was covalently coupled. By this method, serum PAP in a range of 1 to 7,000 ng/ml could be accurately measured within 4 hr.
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