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. 1968 Apr;95(4):1322–1326. doi: 10.1128/jb.95.4.1322-1326.1968

Adenosine Triphosphatase in Isolated Membranes of Staphylococcus aureus

R Gross 1, N W Coles 1
PMCID: PMC315089  PMID: 4230857

Abstract

The preparation of cytoplasmic membranes from suspensions of Staphylococcus aureus lysed by an enzyme recently isolated in these laboratories is described. These membranes contained: protein, 34.4%; ribonucleic acid, 6.6%; lipids, 34.5%; and total phosphorus, 1.4%. Such membranes exhibited adenosine 5′-triphosphatase (E.C. 3.6.1.3) activity, liberating orthophosphate at an initial rate of 0.53 μmole per min per mg of protein under optimal conditions. The enzyme was Mg++-dependent and K+- or Na+-stimulated. Maximal activity was observed with a molar adenosine 5′-triphosphate (ATP) to Mg++ ratio of 1. One mole of orthophosphate was liberated per mole of ATP; the other product of digestion was adenosine 5′-diphosphate. Inorganic pyrophosphate and the 5′-triphosphates of guanosine, uridine, and cytidine were also attacked by membrane preparations, but more slowly than ATP. Ouabain, p-chloromercuribenzoate, and 2,4-dinitrophenol did not alter adenosine triphosphatase activity, whereas both Atebrine and chlorpromazine were inhibitory.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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