Characterization and solubilization of the membrane-bound ATPase of Mycoplasma gallisepticum.

The membrane-bound ATPase of Mycoplasma gallisepticum selectively hydrolyzed purine nucleoside triphosphates and dATP. ADP, although not a substrate, inhibited ATP hydrolysis. The enzyme exhibited a pH optimum of 7.0 to 7.5 and an obligatory requirement for divalent cations. Dicyclohexylcarbodiimide...

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Veröffentlicht in:	J Bacteriol
Hauptverfasser:	Linker, C, Wilson, T H
Format:	Artigo
Sprache:	Inglês
Veröffentlicht:	American Society for Microbiology (ASM) 1985
Schlagworte:	Research Article
Online-Zugang:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC219268/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/3161871/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.163.3.1258-1262.1985
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