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Purification and Characterization of an ATPase GsiA from Salmonella enterica
The coding sequence of Salmonella enterica gsiA was cloned and expressed in E. coli. The protein was purified and ATPase activity was characterized by NADH oxidation method. GsiA exhibited optimum activity at 30°C and at pH 8 in Tris/HCl buffer. GsiA protein was stable at 20°C. 66% and 44% activity...
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| 出版年: | Biomed Res Int |
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| 主要な著者: | , , , |
| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
Hindawi
2017
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| 主題: | |
| オンライン･アクセス: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5485302/ https://ncbi.nlm.nih.gov/pubmed/28691022 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1155/2017/3076091 |
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