J Integr Plant Biol. ›› 1999, Vol. 41 ›› Issue (6): -.

• Research Articles •    

Partial Purification of the Plasma Membrane H+ ATPase from Wheat Roots

QIU Quan-Sheng and SU Xue-Feng   

Abstract: The plasma membrane vesicles were purified from wheat (Triticum aestivum L. ) roots by the sucrose gradient centrifugation methods. Partially purified plasma membrane H+ -ATPases from wheat roots were prepared from the plasma membrane vesicles by a process including Triton X-100 and KC1 treatment, Zwittergent 3-14 solubilization and ammonium sulfate precipitation. The specific activity of H+ -ATPase was increased gradually during purification, and an 8.4 folds increase in ATPase activity was finally obtained. SDS-PAGE showed that the polypeptide of 94 kD was accumulated during the purification and a final content of 15.7 folds increased after the purification. The results indicated that the partially purified plasma membrane H + -ATPases were stimulated by K+ and inhibited by vanadate and N, N'-dicyclohexylcarbodiimide; however, they were not inhibited by NaN3, NaNO3 and Na2MoO4.

Key words: Wheat root, Plasma membrane vesicles, H+ -ATPase purification, Zwittergent 3-14

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