ENZYME ACTIVITY AND BACTERIOPHAGE INFECTION

Author:

Pardee Arthur B.1

Affiliation:

1. From the Virus Laboratory, University of California, Berkeley

Abstract

Experiments have been performed on the apyrase activity of E. coli, strain B. Although the dependence on pH and substrate is similar to that of rat tissue, the bacterial extracts are inhibited by Ca++ and stimulated by Mg++. In bacterial extracts the rate of phosphate release decreases in the course of the reaction, possibly owing to product inhibition. With multiple bacteriophage infection, the apyrase activity of the intact cells increased several fold, and the activity of extracts increased about 30 per cent. It is suggested that the changes could be attributed to an increase in the amount of enzyme although other alternatives cannot be precluded at present.

Publisher

Rockefeller University Press

Subject

Physiology

Cited by 10 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. Kinetic Characteristics of Nucleoside Mono-, Di- and Triphosphatase Activities of the Periplasmic 5′-Nucleotidase of Escherichia coli;Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology;1997-05

2. Thymine Metabolism in Escherichia coli;Journal of Biological Chemistry;1967-04

3. Phosphatases in Bacteriophages T2, T4, and T5;Journal of Biological Chemistry;1959-03

4. Studies on the role of deoxyribonuclease in T2 bacteriophage development;Biochimica et Biophysica Acta;1956-01

5. Apyrase in Partially Purified Staphylococcal Enterotoxin;Journal of Infectious Diseases;1955-05-01

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