The plasma membrane ATPase ofKloeckera apiculata: purification, characterization and effect of ethanol on activity

✍ Scribed by H. Alexandre; C. Charpentier

• Publisher: Springer
• Year: 1994
• Tongue: English
• Weight: 515 KB
• Volume: 10
• Category: Article
• ISSN: 1573-0972
• DOI: 10.1007/bf00327965

✦ Synopsis

Partially (6-fold) purified plasma membrane ATPase from an ethanol-sensitive yeast, Kloeckera apiculata, had an optimum pH of 6.0, an optimum temperature of 35°C, a K m of 3.6 mM ATP and a V max of 11 μmol Pi/min.mg protein. SDS-PAGE of the semi-purified plasma membrane showed a major band of 106 kDa. No in vivo activation of the ATPase by glucose was observed. Although 4% (v/v) ethanol decreased the growth rate by 50% it did not affect the ATPase. Concentrations of ethanol ≥2% (v/v) did, however, inhibit the enzyme in vitro. The characteristics of the enzyme did not change during growth in the presence of ethanol.