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...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Hindawi Limited
2017-01-01
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| Series: | BioMed Research International |
| Online Access: | http://dx.doi.org/10.1155/2017/3076091 |