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. 1984 Nov;76(3):584–588. doi: 10.1104/pp.76.3.584

Characterization and Localization of the ATPase Associated with Pea Chloroplast Envelope Membranes 1

Donald R McCarty 1,2, Kenneth Keegstra 1,2, Bruce R Selman 1,2
PMCID: PMC1064336  PMID: 16663887

Abstract

Chloroplast envelope membranes isolated from Pisum sativum seedlings have been found to contain a Mg-ATPase activity (specific activity 50-175 nanomoles per minute per milligram protein). The ATPase had a broad pH optimum between 7.0 and 9.5. The activity was not inhibited by oligomycin, N,N′-dicyclohexylcarbodiimide, ouabain, or antibodies directed against chloroplast coupling factor 1; nor was the activity stimulated by monovalent cations. However, the ATPase was inhibited by vanadate, molybdate, and adenylyl imidodiphosphate.

The ATPase hydrolyzed a broad range of nucleoside triphosphates, but did not hydrolyze ADP, AMP, or pyrophosphate. The Km for Mg-ATP was determined to be 0.2 millimolar. The ATPase was found to be distinct from ADPase and pyrophosphatase activities also present in pea envelope membranes.

The ATPase was determined to be located on the inner membrane of the envelope after resolution of inner and outer membranes by sucrose density gradient centrifugation.

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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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