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. 1983 Apr;71(4):707–711. doi: 10.1104/pp.71.4.707

Solubilization and Partial Purification of N,N′-Dicyclohexylcarbodiimide-Sensitive ATPase from Pea Cotyledon Mitochondria 1

Mark B Whisson 1, Mary S Spencer 1
PMCID: PMC1066108  PMID: 16662893

Abstract

The N,N′-dicyclohexylcarbodiimide (DCCD)-sensitive ATPase of pea (Pisum sativum L.) cotyledon mitochondria was solubilized from submitochondrial particle membranes with sodium cholate and ammonium sulfate. Ammonium sulfate precipitation of the enzyme resulted in an increase in specific activity. At between 38% and 45% saturated ammonium sulfate, 20% of the ATPase activity was precipitated, with a specific activity 4 to 5 times higher than that of the crude enzyme. The precipitate was highly sensitive to DCCD.

The properties of the ammonium sulfate preparation were investigated. It contained levels of cytochrome and NADH dehydrogenase contamination comparable to those of the highly purified F0F1 preparations from animal tissue. The high degree of purification was corroborated by sodium dodecyl sulfate electrophoresis.

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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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