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

Author:

Foti Andras G1,Herschman Harvey2,Cooper J Fenimore3,imFeld Hedi1

Affiliation:

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

Abstract

Abstract 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.

Publisher

Oxford University Press (OUP)

Subject

Biochemistry, medical,Clinical Biochemistry

Cited by 5 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

1. Developments in the chemistry and applications of phthalein dyes. Part 2: biological applications;Coloration Technology;2018-07-09

2. Further Studies on Human Testicular Acid Phosphatases;Andrologia;2009-04-24

3. T;Handbook of Acid-Base Indicators;2007-10-04

4. Biochemistry of Prostatic Carcinoma;Biochemical and Molecular Aspects of Selected Cancers;1994

5. Acid Phosphatases of the Human Testis Separation and Enzyme Characteristics;International Journal of Andrology;1980-12

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