Maria Cecilia Cocucci, Maria Ida De Michelis, Maria Chiara Pugliarello, Franca Rasi-Caldogno
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Reconstitution of proton pumping activity of a plasma membrane ATPase purified from radish
Plasma membrane ATPase partially purified from radish seedlings (Raphanus sativum L.) (2.4–3.5 μmol Pi min−1 mg−1 protein) has been reconstituted in proteoliposomes by the cholate-dialysis technique. Proteoliposomes are able to acidify their internal volume in the presence of Mg:ATP. Mg:ATP-dependent proton pumping is prevented by N,N′-dicyclohexylcarbodiimide (DCCD) and by vanadate at the same concentrations which are effective on the phosphohydrolyzing activity of the plasma membrane ATPase.
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