Membranes prepared from various members of the genus Halobacterium contained a Triton X-100 activated adenosine triphosphatase. The enzyme from Halobacterium saccharovorum was unstable in solutions of low ionic strength (< 3 M NaCl) and maximally active in the presence of 3.5 M NaCl. A variety of nucleotide triphosphates was hydrolyzed. MgADP, the product of ATP hydrolysis, was not hydrolyzed and was a competitive inhibitor with respect to MgATP. The enzyme from H. saccharovorum was composed of at least 2 and possibly 4 subunits. The 83-kDa and 60-kDa subunits represented about 90% of total protein. The 60-kDa subunit reacted with dicyclohexylcarbodiimide (DCCD) when inhibition was carried out in an acidic medium. The significance of the two minor components (28 kDa and 12 kDa is not established. The enzyme from H. saccharovorum, which differs from previously described halobacterial ATPases, possesses properties of an F1F0 as well as an E1E2 ATPase.

中文翻译：

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嗜盐细菌嗜盐杆菌中的卤代细菌腺苷三磷酸酶和腺苷三磷酸酶。

由盐杆菌属的各个成员制备的膜包含Triton X-100活化的腺苷三磷酸酶。在低离子强度（<3 M NaCl）的溶液中，来自嗜盐杆菌的酶不稳定，并且在存在3.5 M NaCl的情况下具有最大活性。各种核苷酸三磷酸被水解。ATP水解的产物MgADP未被水解，相对于MgATP是竞争性抑制剂。酿酒酵母的酶由至少2个，可能是4个亚基组成。83-kDa和60-kDa亚基约占总蛋白的90％。当在酸性介质中进行抑制时，60 kDa亚基与二环己基碳二亚胺（DCCD）反应。尚未确定两个次要成分（28 kDa和12 kDa）的重要性。