Kubak B M, Yotis W W
J Bacteriol. 1981 Apr;146(1):385-90. doi: 10.1128/jb.146.1.385-390.1981.
Homogeneous preparations of cytoplasmic membrane isolated from Staphylococcus aureus 6538P exhibited membrane-associated adenosine triphosphatase (ATPase) activity. Membrane ATPase activity was activated by divalent cations (4.0 mM: Mg2+ greater than Mn2+ greater than Co2+ greater than Zn2+), and ATP was hydrolyzed more readily than other nucleoside triphosphates and phosphorylated substrates. The pH optimum for the membrane ATPase was 6.5. The ATPase could not be released from the membrane by differential osmotic treatments, but detergent treatment effectively solubilized active enzyme. The nonionic detergent Triton X-100 (1%) released a protein with ATPase activity, after substrate-dependent staining in polyacrylamide gels, that differed slightly in electrophoretic migration when compared to the active enzyme solubilized with sodium dodecyl sulfate (0.1%). Membrane-associated ATPase activity was inhibited by N,N'-dicyclohexylcarbodiimide (0.001 to 1 mM) and NaF (50% inhibition at 5 mM NaF). Azide and trypsin inhibited activity, whereas ouabain had a slight inhibitory effect. Diethylstilbestrol showed appreciable activation of the membrane ATPase over the range employed (0.001 to 1 mM).
从金黄色葡萄球菌6538P分离得到的细胞质膜均一制剂表现出与膜相关的腺苷三磷酸酶（ATP酶）活性。膜ATP酶活性被二价阳离子激活（4.0 mM：Mg2+＞Mn2+＞Co2+＞Zn2+），并且ATP比其他核苷三磷酸和磷酸化底物更易被水解。膜ATP酶的最适pH为6.5。通过不同的渗透处理不能使ATP酶从膜上释放，但去污剂处理可有效地溶解活性酶。非离子去污剂Triton X-100（1%）在聚丙烯酰胺凝胶中经底物依赖性染色后释放出具有ATP酶活性的一种蛋白质，与用十二烷基硫酸钠（0.1%）溶解的活性酶相比，其电泳迁移率略有不同。膜相关ATP酶活性被N，N'-二环己基碳二亚胺（0.001至1 mM）和NaF（在5 mM NaF时50%抑制）抑制。叠氮化物和胰蛋白酶抑制活性，而哇巴因有轻微抑制作用。己烯雌酚在所采用的浓度范围（0.001至1 mM）内对膜ATP酶有明显的激活作用。
