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Clinical Chemistry 21: 1761-1765, 1975;
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Clinical Chemistry, Vol 21, 1761-1765, Copyright © 1975 by the American Association for Clinical Chemistry

Enhancing Effect of Surfactant and Protein on Hydrolysis of Thymolphthalein Monophosphate by Purified Prostatic Acid Phosphatase

Andras G. Foti 1, Harvey Herschman 2, J. Fenimore Cooper 3, and Hedi imFeld 1

1 Department of Research, Southern California Permanente Medical Group, Los Angeles, Calif. 90027.
2 Department of Biological Chemistry and Laboratory of Nuclear Medicine, UCLA School of Medicine, Los Angeles, Calif. 90024.
3 Department of Urology, Southern California Permanente Medical Group and Kaiser Foundation Hospital, Los Angeles, Calif. 90027.

Purified prostatic acid phosphatase catalyzes the hydrolysis of thymolphthalein monophosphate 10-fold faster if an optimal concentration of Brij 35 (a wetting agent) or protein (bovine serum albumin or human serum proteins) is present. Results of gel filtration, dialysis, and sucrose density-gradient centrifugation analysis suggest that the substrate must combine with detergent or protein before the enzyme can catalyze its hydrolysis.

Submitted on June 9, 1975
Accepted on August 19, 1975






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Copyright © 1975 by the American Association for Clinical Chemistry.