部分纯化的醋化醋杆菌膜中的 ATP 酶活性。
ATPase activities in partially purified membranes of Acetabularia.
机构信息
Max-Planck-Institut für Biochemie, D-8033, Martinsried, FRG.
出版信息
Plant Cell Rep. 1983 Jun;2(3):152-5. doi: 10.1007/BF00269342.
Partly purified membranes (with plasmalemma material) of Acetabularia mediterranea were studied with respect to ATPase activity in alkali- and Ca(++)-free media and its sensitivity to pH (5 - 9), oligomycin (200 ώg/mg protein), 100 ώM N-N'-dicyclohexylcarbodiimide (DCCD), and 50 ώM vanadate. Besides activities which may originate from mitochondrial H(+) ATPase (oligomycin-sensitive, alkaline pH optimum) and tonoplast H(+) ATPase (DCCD-sensitive, pH optimum 7.5), there is ATPase activity with a pH optimum around pH 6.5, sensitive to vanadate and insensitive to DCCD. These results strongly suggest that the electrogenic Cl(-) pump in the plasmalemma of Acetabularia is an ATPase. Effects of Mg(++), Mg-ATP, ADP, GTP, UTP, CTP and HCO3 (-) versus Cl(-) on this ATPase activity are described.
对半纯化的地中海扇贝多肽膜（质膜材料）在碱性和无钙介质中的 ATP 酶活性及其对 pH 值（5-9）、寡霉素（200μg/mg 蛋白）、100μM N-N'-二环己基碳二亚胺（DCCD）和 50μM 钒酸盐的敏感性进行了研究。除了可能源于线粒体 H(+)ATP 酶（寡霉素敏感，碱性 pH 值最佳）和液泡膜 H(+)ATP 酶（DCCD 敏感，pH 值最佳 7.5）的活性外，还有一种 pH 值最佳约为 pH6.5 的 ATP 酶活性，对钒酸盐敏感，对 DCCD 不敏感。这些结果强烈表明，地中海扇贝多肽质膜中的电致 Cl(-)泵是一种 ATP 酶。描述了 Mg(++)、Mg-ATP、ADP、GTP、UTP、CTP 和 HCO3(-)对这种 ATP 酶活性的影响与 Cl(-)的关系。
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