膜结合三磷酸腺苷酶的免疫学特性：通过交叉免疫电泳对藤黄微球菌ATCC 4698中鲁塔霉素敏感的F0.F1ATP酶进行免疫学鉴定。

Immunological properties of membrane-bound adenosine triphosphatase: immunological identification of rutamycin-sensitive F0.F1ATPase from Micrococcus luteus ATCC 4698 established by crossed immunoelectrophoresis.

作者信息

Schmitt M, Rittinghaus K, Scheurich P, Schwulera U, Dose K

出版信息

Biochim Biophys Acta. 1978 Jun 2;509(3):410-8. doi: 10.1016/0005-2736(78)90235-3.

Abstract

(1) F0.F1ATPase (EC 3.6.1.3) from Micrococcus luteus ATCC 4698 was solubilized from plasma membranes by the non-ionic detergent Triton X-100 in the presence of 0.05 M MgCl2. (2) The antibiotics rutamycin, Dio-9, quercetin, oligomycin, botrycidin, efrapeptin, leucinostatin, valinomycin, and venturicidin as well as N,N'-dicyclohexylcarbodiimide and dinitrophenol are potent inhibitors of F0.F1ATPase activity.(3) F0.F1ATPase activity is completely inhibited by anti-F1ATPase antibodies. The inhibition is non-competitive. (4) Crossed immunoelectrophoresis reveals a reaction of immunological identity of F0.F1ATPase and F1ATPase indicating that both enzymes have in common antigenic sites.

摘要

(1) 来自藤黄微球菌ATCC 4698的F0.F1ATP酶（EC 3.6.1.3）在0.05 M氯化镁存在的情况下，通过非离子型去污剂曲拉通X-100从质膜中溶解出来。(2) 抗生素鲁塔霉素、Dio-9、槲皮素、寡霉素、杀稻瘟菌素、埃弗拉菌素、亮抑酶肽、缬氨霉素、抗霉素以及N,N'-二环己基碳二亚胺和二硝基苯酚是F0.F1ATP酶活性的有效抑制剂。(3) F0.F1ATP酶活性被抗F1ATP酶抗体完全抑制。这种抑制是非竞争性的。(4) 交叉免疫电泳显示F0.F1ATP酶和F1ATP酶具有免疫同一性反应，表明这两种酶具有共同的抗原位点。