Plant Physiol.
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Plant Physiology 70:1115-1119 (1982)
© 1982 American Society of Plant Biologists

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Localization of a Proton-Translocating ATPase on Sucrose Gradients 1

Frances M. Dupont2, Alan B. Bennett and Roger M. Spanswick

Section of Plant Biology, Division of Biological Science, Plant Science Building, Cornell University, Ithaca, New York 14853

Ionophore-stimulated ATPase activity and ATP-dependent quinacrine quench were enriched in parallel when microsomal vesicles were prepared from corn (Crow Single Cross Hybrid WF9-Mo17) roots and collected on a cushion of 10% dextran. Activities were highest in the apical 1.5 centimeters of the roots. Vesicles collected on the dextran cushion also contained NADH cytochrome c reductase (enriched in the apical 0.5 cm of the root) and nucleoside diphosphatase (distributed throughout the first four cm). On continuous sucrose gradients, ATP-dependent proton transport and ionophore-stimulated ATPase activity coincided in a broad band extending from 1.08 to 1.15 grams per cubic centimeter with maximum activity at 1.10 to 1.12 grams per cubic centimeter. Large portions of the proton-translocating ATPase activity and ionophore-stimulated ATPase activity were clearly separable from mitochondrial membranes containing cytochrome c oxidase activity and azide-sensitive, pH 8.5 ATPase activity and from membranes bearing {beta}-glucan synthetase I and II. The vesicles coincided with a minor portion of the NADH-cytochrome c reductase and nucleoside diphosphatase activities. It is suggested that the vesicles are of tonoplast origin.

2 Present address: ARCO Plant Cell Research Institute, 6560 Trinity Court, Dublin, CA 94568.

1 Supported by Grant PCM 78-12119 from the National Science Foundation to R. M. S.




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K. W. Beyenbach and H. Wieczorek
The V-type H+ ATPase: molecular structure and function, physiological roles and regulation
J. Exp. Biol., February 15, 2006; 209(4): 577 - 589.
[Abstract] [Full Text] [PDF]


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Copyright © 1982 by the American Society of Plant Biologists