Plant Physiol.
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Plant Physiology 65:281-285 (1980)
© 1980 American Society of Plant Biologists

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Articles

ATPase Activity of Pea Cotyledon Submitochondrial Particles

ACTIVATION, SUBSTRATE SPECIFICITY, AND ANION EFFECTS 1

Charles Grubmeyer2 and Mary Spencer3

Department of Plant Science, University of Alberta, Edmonton, Alberta T6G 2E3 Canada

Submitochondrial particles freshly prepared by sonication from pea cotyledon mitochondria showed low ATPase activity. Activity increased 20-fold on exposure to trypsin. The pea cotyledon submitochondrial particle ATPase was also activated by "aging" in vitro. At pH 7.0 addition of 1 millimolar ATP prevented the activation. ATPase of freshly prepared pea cotyledon submitochondrial particles had a substrate specificity similar to that of the soluble ATPase from pea cotyledon mitochondria, with GTPase > ATPase. "Aged" or trypsin-treated particles showed equal activity with the two substrates. NaCl and NaHCO3, which stimulate the ATPase but not the GTPase activity of the soluble pea enzyme, were stimulatory to both the ATPase and GTPase activities of freshly prepared submitochondrial particles. However, they were stimulatory only to the ATPase activity of trypsin-treated or "aged" submitochondrial particles. In contrast, the ATPase activity of rat liver submitochondrial particles was stimulated by HCO3–, but inhibited by Cl–, indicating that Cl– stimulation is a distinguishing property of the pea mitochondrial ATPase complex.

2 Present address: Public Health Research Institute, 455 First Avenue, New York, New York 10016.

3 To whom requests for reprints should be addressed.

1 This work was supported by the National Research Council of Canada through a grant-in-aid (A-1451), and a Postgraduate Scholarship for C. G.






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Copyright © 1980 by the American Society of Plant Biologists