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Plant Physiology 81:126-129 (1986)
© 1986 American Society of Plant Biologists

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Chromatographic Resolution of H+-Translocating Pyrophosphatase from H+-Translocating ATPase of Higher Plant Tonoplast 1

Philip A. Rea2 and Ronald J. Poole

Department of Biology, McGill University, Montreal, Quebec, CANADA H3A 1B1

Membrane vesicles derived from the tonoplast of Beta vulgaris L. possess two predominant phosphohydrolase activities: a Cl–-stimulated, NO3–-inhibited ATPase, and a K+-stimulated, Na+-inhibited inorganic pyrophosphatase (PPase). The solubilization of tonoplast vesicles with 2% (w/v) Triton X-100 containing 4 millimolar MgCl2 and 1 millimolar ethylenediamine tetracetic acid, as protectants, gives high yields of both the ATPase and PPase in soluble form. Chromatography of the solubilized membranes on Sephacryl-400 results in the separation of the two enzymes. The PPase and ATPase are purified 4- and 17-fold, respectively, with quantitative recovery. The separated enzymes show negligible activity towards the other's substrate and the separated PPase only hydrolyzes pyrophosphate. The separated enzymes show mineral ion requirements identical to those of the corresponding pump and hydrolytic activities in native tonoplast and both solubilized enzymes are subject to phospholipid activation.

2 Address for correspondence: Department of Biology, University of York, Heslington, York YO1 5DD, England.

1 Supported by the Natural Sciences and Engineering Research Council of Canada and the Department of Education of Quebec.




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Copyright © 1986 by the American Society of Plant Biologists