Two forms of yeast plasma membrane H(+)-ATPase: comparison of yield and effects of inhibitors
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
11271804
DOI
10.1007/bf02908948
Knihovny.cz E-zdroje
- MeSH
- adenosintrifosfát metabolismus MeSH
- buněčná membrána enzymologie MeSH
- inhibitory enzymů farmakologie MeSH
- kultivační média MeSH
- protonové ATPasy antagonisté a inhibitory izolace a purifikace metabolismus MeSH
- Saccharomyces cerevisiae enzymologie růst a vývoj MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- adenosintrifosfát MeSH
- inhibitory enzymů MeSH
- kultivační média MeSH
- protonové ATPasy MeSH
Classical isolation procedure for plasma membrane H(+)-ATPase of Saccharomyces cerevisiae based on fractional centrifugation yielded always a roughly two-fold greater amount of membranes when starting from glucitol-preincubated than from glucose-preincubated yeast. This difference persisted all the way to the purified plasma membranes and to the purified H(+)-ATPase. The ATP-hydrolyzing activity by plasma membranes was roughly twice greater in glucose-preincubated cells than in the D-glucitol-preincubated ones while the purified enzyme was 7 times more active after glucose than after glucitol. Effects of diethylstilbestrol, suloctidil, erythrosin B, vanadate and dicarbanonaboranuide were very similar on plasma membrane-localized and purified ATPases of both forms, suggesting that both preparations contain the two ATPase forms, the glucose-preincubated one being richer in the activated form while the glucitol-preincubated one contains less of it.
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