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. 1979 Nov;140(2):745–747. doi: 10.1128/jb.140.2.745-747.1979

Properties and function of the proton-translocating adenosine triphosphatase of Clostridium perfringens.

S M Hasan, B P Rosen
PMCID: PMC216707  PMID: 40963

Abstract

Growth of Clostridium perfringens was inhibited by compounds which dissipate or prevent the formation of electrochemical proton gradients. Membrane vesicles prepared from this organism exhibited Mg2+-dependent adenosine triphosphatase (ATPase) activity sensitive to N,N'-dicyclohexylcarbodiimide. Mg2+-ATPase activity was optimal of 50 degrees C, but no discrete pH optimum was observed. Adenosine triphosphate-dependent quenching of the fluorescence of the weak base quinacrine by everted membrane vesicles suggested that the Mg2+-ATPase is a proton pump capable of generating an electrochemical proton gradient. Adenosine triphosphate-dependent transport of Ca2+ by everted vesicles was sensitive to uncouplers and inhibitors of the Mg2+-ATPase.

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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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