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支原体中活性(F1-F0)-ATP酶的免疫化学证据。

Immunochemical evidence for an active (F1-F0)-ATPase in mycoplasmas.

作者信息

Rottem S, Shirvan M H, Barile M F, Zilberstein D

机构信息

Department of Membrane and Ultrastructure Research, Hebrew University-Hadassah Medical School, Jerusalem, Israel.

出版信息

Isr J Med Sci. 1987 May;23(5):389-92.

PMID:2889695
Abstract

In all Acholeplasma, Mycoplasma and Spiroplasma species tested, a protein capable of reacting with antibodies prepared against the beta subunit of the proton-ATPase complex from yeast, chloroplasts and Escherichia coli was detected. The reactive protein of M. gallisepticum was found to be catalytically active, suggesting that mycoplasmas, as other bacteria, possess a proton-translocating ATPase. Characterization of the ATPase activity of M. gallisepticum indicates that this organism also possesses a Na+-stimulated ATPase activity that differs from the proton-ATPase in its pH profile and its resistance to dicyclohexylcarbodiimide (DCCD).

摘要

在所有检测的无胆甾原体属、支原体属和螺原体属物种中,均检测到一种能与针对酵母、叶绿体和大肠杆菌质子 - ATP酶复合体β亚基制备的抗体发生反应的蛋白质。发现鸡毒支原体的反应性蛋白质具有催化活性,这表明支原体与其他细菌一样,拥有一种质子转运ATP酶。对鸡毒支原体ATP酶活性的表征表明,该生物体还具有一种受Na⁺刺激的ATP酶活性,其在pH曲线和对二环己基碳二亚胺(DCCD)的抗性方面与质子 - ATP酶不同。

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