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Plant and Cell Physiology, 1986, Vol. 27, No. 1 49-59
© 1986

Article

Comparison of Plasma Membrane and Tonoplast H+-Translocating ATPases in Phaseolus mungo L. Roots

Kunihiro Kasamo

Department of Cell Biology, National Institute of Agrobiological Resources Tsukuba Science City, Yatabe, Ibaraki 305, Japan

Two membrane fractions were obtained from 16%/26% and 34%/40% interfaces following discontinuous sucrose density gradient centrifugation of a 10,000–80,000xg pellet from mung bean (Phaseolus mungo L.) roots. The ATPases in the fractions differed from each other in their sensitivity toward various inhibitors, activation with salts, dependence of activity on pH, and Km for ATP.Mg2+. Judging from their sensitivity toward inhibitors, the ATPases in the low and high density membranes are considered mainly of tonoplast and plasma membrane origin, respectively. Both ATPases were activated by gramicidin D and nigericin. ATP-induced quenching of quinacrine fluorescence in both fractions required Mg2+ and permeant anions such as Cl– and quenching was collapsed by carbonylcyanide p-trifluoromethoxyphenyl hydrazone. The sensitivities of quenching to the inhibitors were essentially the same as those of ATPase activity in the membranes. These findings suggest the involvement of ATPases in H+-pumping across a plasma membrane and tonoplast.

(Received April 12, 1985; Accepted October 11, 1985)
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