Purification and Properties of the Plasma Membrane H+-Translocating Adenosine Triphosphatase of Phaseolus mungo L. Roots
Open Access
- 1 April 1986
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 80 (4) , 818-824
- https://doi.org/10.1104/pp.80.4.818
Abstract
The plasma membrane ATPase of mung bean (Phaseolus mungo L.) roots has been solubilized with a two-step procedure using the anionic detergent, deoxycholate (DOC) and the zwitterionic detergent, zwittergent 3-14 as follows: (a) loosely bound membrane proteins are removed by treatment with 0.1% DOC; (b) The ATPase is solubilized with 0.1% zwittergent in the presence of 1% DOC; (c) the solubilized material is further purified by centrifugation through a glycerol gradient (45-70%). Typically, about 10% of the ATPase activity is recovered, and the specific activity increases about 11-fold. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis shows that the peak fraction from the glycerol gradient contains three major polypeptides of Mr = 105,000, 67,000, and 57,000 daltons. The properties of the purified ATPase are essentially the same as those of membrane-bound ATPase, with respect to pH optimum, substrate specificity, inhibitor sensitivity, and ion stimulation.This publication has 29 references indexed in Scilit:
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