ENZYME ACTIVITY AND BACTERIOPHAGE INFECTION
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چکیده
منابع مشابه
Enzyme Activity and Bacteriophage Infection
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...
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In previous communications we have brirfly dcscribrd the properties of a dcoxycytidine triphosphate-cleaving enzyme (deoxycytidine triphosphatase) which appears in Escherichia coli cells after infection with bacteriophage T2 (1, 2). The prcscnce of this enzyme was first noted because of its property of excluding dCTP’ as a substrate for the deoxyribonucleic acid polymerase present in cell-free ...
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The activities of six bacteriophage T2r+-induced enzymes (thymidylate synthetase, deoxycytidylate deaminase, thymidylate kinase, deoxycytidylate hydroxymethylase, deoxycytidine pyrophosphatase, and dihydrofolate reductase) were measured after dilution of phage-infected Escherichia coli B from 8 X 108 to 2 x 108 cells per ml. The only enzyme activity altered was that of deoxycytidylate deaminase...
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In an earlier report dealing with the chemistry of viral invasion, Barrington and Kozloff (1,2) showed that incubat,ion of various T series bacteriophages with N16-labeled Escherichiu coli B cell walls caused the release of as much as 15 per cent of the total nitrogen from the host cell walls. The characteristics of this interaction appeared to be similar to those of an enzymatic reaction, and ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1952
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)44806-5