Nejvíce citovaný článek - PubMed ID 2906716
The plasma membrane H(+)-ATPase activity was determined under various growth conditions using the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe. Under early batch-growth conditions in a rich medium, the budding yeast S. cerevisiae ATPase specific activity increased 2- to 3-fold during exponential growth. During late exponential growth, a peak of ATPase activity, followed by a sudden decrease, was observed and termed "growth-arrest control". The growth arrest phenomenon of S. cerevisiae could not be related to the acidification of the culture medium or to glucose exhaustion in the medium or to variation of glucose activation of the H(+)-ATPase. Addition of ammonium to a proline minimum medium also stimulated transiently the ATPase activity of S. cerevisiae. Specific activity of the fission yeast S. pombe ATPase did not show a similar profile and steadily increased to reach a plateau in stationary growth. Under synchronous mitotic growth conditions, the ATPase activity of S. cerevisiae increased during the cell division cycle according to the "peak" type cycle, while that of S. pombe was of the "step" type.
- MeSH
- buněčná membrána enzymologie MeSH
- glukosa metabolismus MeSH
- kinetika MeSH
- kultivační média MeSH
- protonové ATPasy metabolismus MeSH
- Saccharomyces cerevisiae enzymologie růst a vývoj MeSH
- Schizosaccharomyces enzymologie růst a vývoj MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- glukosa 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.
- 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
