Laboratoire d'Oenologie, Institut Universitaire de la Vigne et du Vin, Université de Bourgogne, BP 138, 21004, Dijon cedex, France.
World J Microbiol Biotechnol. 1994 Nov;10(6):704-8. doi: 10.1007/BF00327965.
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.
从乙醇敏感酵母 Kloeckera apiculata 中部分（6 倍）纯化的质膜 ATP 酶在 pH6.0 时具有最佳活性，最适温度为 35°C，Km 值为 3.6mM ATP，Vmax 值为 11μmol Pi/min.mg 蛋白。半纯化质膜的 SDS-PAGE 显示出 106kDa 的主要条带。没有观察到葡萄糖对 ATP 酶的体内激活。虽然 4%（v/v）乙醇使生长速率降低了 50%，但它不影响 ATP 酶。然而，乙醇浓度≥2%（v/v）确实会抑制体外酶的活性。在乙醇存在下生长时，酶的特性没有改变。
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