Reconstitution of proton pumping activity of a plasma membrane ATPase purified from radish
1985; Elsevier BV; Volume: 37; Issue: 3 Linguagem: Inglês
10.1016/0304-4211(85)90002-1
ISSN1878-2310
AutoresMaria Cecilia Cocucci, Maria Ida De Michelis, Maria Chiara Pugliarello, Franca Rasi‐Caldogno,
Tópico(s)Photosynthetic Processes and Mechanisms
ResumoPlasma 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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