Maria Cecilia Cocucci, Maria Ida De Michelis, Maria Chiara Pugliarello, Franca Rasi-Caldogno
{"title":"Reconstitution of proton pumping activity of a plasma membrane ATPase purified from radish","authors":"Maria Cecilia Cocucci, Maria Ida De Michelis, Maria Chiara Pugliarello, Franca Rasi-Caldogno","doi":"10.1016/0304-4211(85)90002-1","DOIUrl":null,"url":null,"abstract":"<div><p>Plasma membrane ATPase partially purified from radish seedlings (<em>Raphanus sativum</em> L.) (2.4–3.5 μmol P<sub>i</sub> min<sup>−1</sup> mg<sup>−1</sup> 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 <em>N</em>,<em>N</em>′-dicyclohexylcarbodiimide (DCCD) and by vanadate at the same concentrations which are effective on the phosphohydrolyzing activity of the plasma membrane ATPase.</p></div>","PeriodicalId":20221,"journal":{"name":"Plant Science Letters","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0304-4211(85)90002-1","citationCount":"16","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Plant Science Letters","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0304421185900021","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 16
Abstract
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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