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首页> 外文期刊>Journal of bacteriology >Purification and Properties of the F1Fo ATPase of Ilyobacter tartaricus, a Sodium Ion Pump
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Purification and Properties of the F1Fo ATPase of Ilyobacter tartaricus, a Sodium Ion Pump

机译：钠离子泵Itaryotar tariaricus F1Fo ATPase的纯化和性质

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The ATPase of Ilyobacter tartaricus was solubilized from the bacterial membranes and purified. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified enzyme revealed the usual subunit pattern of a bacterial F1Fo ATPase. The polypeptides with apparent molecular masses of 56, 52, 35, 16.5, and 6.5 kDa were identified as the α, β, γ, ?, and c subunits, respectively, by N-terminal protein sequencing and comparison with the sequences of the corresponding subunits from the Na+-translocating ATPase ofPropionigenium modestum. Two overlapping sequences were obtained for the polypeptides moving with an apparent molecular mass of 22 kDa (tentatively assigned as b and δ subunits). No sequence could be determined for the putative a subunit (apparent molecular mass, 25 kDa). The c subunits formed a strong aggregate with the apparent molecular mass of 50 kDa which required treatment with trichloroacetic acid for dissociation. The ATPase was inhibited by dicyclohexyl carbodiimide, and Na+ ions protected the enzyme from this inhibition. The ATPase was specifically activated by Na+ or Li+ ions, markedly at high pH. After reconstitution into proteoliposomes, the enzyme catalyzed the ATP-dependent transport of Na+, Li+, or H+. Proton transport was specifically inhibited by Na+ or Li+ ions, indicating a competition between these alkali ions and protons for binding and translocation across the membrane. These experiments characterize the I. tartaricus ATPase as a new member of the family of FS-ATPases, which use Na+ as the physiological coupling ion for ATP synthesis.
机译：从细菌膜中溶解并纯化了 tartaricus 的ATPase。纯化的酶的十二烷基硫酸钠-聚丙烯酰胺凝胶电泳显示细菌F 1 F o ATP酶的常见亚基模式。通过N端蛋白质测序并与相应的序列进行比较，分别将表观分子量为56、52、35、16.5和6.5 kDa的多肽分别鉴定为α，β，γ，γ和c亚基。幽门螺旋菌的Na + 易位ATPase的两个亚基。对于以22kDa的表观分子量（暂定为b和δ亚基）移动的多肽，获得了两个重叠序列。无法确定推定的亚基的序列（表观分子量，25 kDa）。 c个亚基形成强聚集体，其表观分子量为50 kDa，需要用三氯乙酸处理使其解离。 ATPase被二环己基碳二亚胺抑制，而Na + 离子保护该酶免受这种抑制。 ATPase被Na + 或Li + 离子特异性激活，在高pH值下显着。重组为蛋白脂质体后，该酶催化Na + ，Li + 或H + 的ATP依赖性转运。 Na + 或Li + 离子可特异性抑制质子运输，表明这些碱离子与质子之间的竞争是通过膜的结合和转运。这些实验表征了 I。 art（tartaricus） ATPase是FS-ATPase家族的一个新成员，该家族使用Na + 作为ATP合成的生理耦合离子。

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