Plant Physiol.
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Plant Physiology 71:707-711 (1983)
© 1983 American Society of Plant Biologists

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Articles

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

Mark B. Whisson and Mary S. Spencer

Department of Plant Science, University of Alberta, Edmonton, Alberta T6G 2P5 Canada

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.

1 Supported by grant S-1451 to M. S. S. from the Natural Sciences and Engineering Council of Canada. M. B. W. was the recipient of a University of Alberta Graduate Research Assistantship.






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Copyright © 1983 by the American Society of Plant Biologists