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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| Опубликовано в:: | J Bacteriol |
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| Главные авторы: | , |
| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
American Society for Microbiology (ASM)
1985
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| Предметы: | |
| Online-ссылка: | 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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