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[Cancer Research 27, 148-151, January 1, 1967]
© 1967 American Association for Cancer Research

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Studies on Latent Derivatives of Aminoethanethiols as Potentially Selective Cytoprotectants

IV. Enzymatic Hydrolysis of Cysteamine-S-phosphate1

Katherine A. Herrington, Carolyn J. Small, Alton Meister2 and Orrie M. Friedman

Collaborative Research, Inc., Waltham, Massachusetts

Rat liver homogenates catalyze the hydrolysis of cysteamine-S-phosphate to cysteamine and orthophosphate. The reaction, which is stimulated by magnesium ions, occurs at maximal rate between pH 8 and 9. Of a number of rat tissues examined, kidney, duodenum, and liver were most active. No activity was found in blood serum. The ratio of the hydrolytic activities of these tissues toward cysteamine-S-phosphate and p-nitrophenylphosphate was fairly constant, with the notable exceptions of liver and blood serum. Cysteamine-S-phosphate is hydrolyzed rapidly by a highly purified preparation of calf intestinal alkaline phosphatase.

1 Supported by a research contract, PH43-62-170, Cancer Chemotherapy National Service Center, National Cancer Institute, NIH, Bethesda, Md.

2 Department of Biochemistry, Tufts University School of Medicine, Boston, Mass.

Received 5/ 3/66. Accepted 8/19/66.







HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Cancer Research Clinical Cancer Research
Cancer Epidemiology Biomarkers & Prevention Molecular Cancer Therapeutics
Molecular Cancer Research Cancer Prevention Research
Cancer Prevention Journals Portal Cancer Reviews Online
Annual Meeting Education Book Meeting Abstracts Online
Copyright © 1967 by the American Association for Cancer Research.