Reconstitution of Plasma Membrane ATPase from Mature Cucumber Roots

概要

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ATPase was solubilized with n-octylglucoside from plasma membrane-enriched fractions of mature cucumber roots. Partially purified ATPase was prepared by the centrifugation of an n-octylglucoside dilution method. Equilibrium density centrifugation showed that the densities of ATPase reconstituted into proteoliposomes and of ATPase from the native plasma membrane-enriched fraction detected by ATPase activity were 1.115 and 1.175 g cm^<-3>, respectively. The ATPase reconstituted into proteoliposomes showed a high specificity for ATP as a substrate, while other nucleotides, pyrophosphate and p-nitorophenyl-phosphate were hardly hydrolyzed. The optimum pH of the reconstituted ATPase was 6.0 and the K_m value for ATP was 0.23 mol m^<-3>. The reconstituted ATPase was activated by various monovalent cations accompanying chloride anion but not by choline chloride. Various potassium salts activated the reconstituted ATPase. As a whole, ATPase reconstituted into proteoliposomes through simple procedures showed typical characteristics of plasma membrane type ATPase.
一般社団法人日本土壌肥料学会の論文
1993-03-00