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Partial purification of a dicyclohexylcarbodi-imide-sensitive membrane adenosine triphosphatase complex from the obligately anaerobic bacterium Clostridium Pasteurianum.

ABSTRACT: The membrane adenosine triphosphatase complex of vegetatively growing Clostridium pasteurianum, solublized with Triton X-100, has been recovered as a significantly purified particulate preparation that is still sensitive to inhibition by dicyclohexylcarbodiimide and butyricin 7423.

SUBMITTER: Clarke DJ

PROVIDER: S-EPMC1172775 | biostudies-other | 1976 Mar

REPOSITORIES: biostudies-other

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Inhibition of the membrane-bound adenosine triphosphatase of Escherichia coli by dicyclohexylcarbodi-imide.

Project description:The inhibition of the membrane-bound adenosine triphosphatase of Escherichia coli by DCCD (dicyclohexylcarbodi-imide) is studied under conditions of varying KCl concentration. An increase in K+ concentration and in other cations causes an increase in the DCCD sensitivity of the enzyme, as well as significant changes in the kinetic parameters.

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The mother-cell-membrane adenosine triphosphatase of sporulating Clostridium pasteurianum.

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Closed Genome Sequence of Clostridium pasteurianum ATCC 6013.

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