HUMAN PROSTATIC ACID-PHOSPHATASES - PURIFICATION OF A MINOR ENZYME AND COMPARISONS OF THE ENZYMES

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  • 1 January 1979
    • journal article
    • research article
    • Vol. 16  (5) , 349-352
Abstract
The minor enzyme of human prostatic acid phosphatases (pI 5.5) with high specific activity (orthophosphoric monoester phosphohydrolase, acid optimum, EC 3.1.3.2) was purified for the 1st time as a pure enzyme protein. The enzyme was a single protein when examined by polyacrylamide gel electrophoresis and isotachophoresis. The specific activity was 1080 .mu.mol/(min .times. mg) for hydrolysis of 5.5 mmol/l of p-nitrophenylphosphate at pH 4.8 and 37.degree. C. The purification coefficient was 540 and the recovery of enzyme activity was 2%. The MW of the enzyme subunit when measured by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate was 54,000. The Km of the purified enzyme was 3 .times. 10-4 mol/l for p-nitrophenylphosphate. An antiserum to this enzyme was prepared. The enzyme was cross-reactive with the main enzyme (pI 4.9) of human prostatic acid phosphatases in immunoelectrophoresis. No precipitin arc with the acid phosphatase in the serum of a prostatic carcinoma patient could be shown. Antiserum to the main enzyme caused a precipitin line with the same serum sample.

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