Purification and characterization of the F1-ATPase from Clostridium thermoaceticum.
The F1 portion of the H+-ATPase from Clostridium thermoaceticum was purified to homogeneity by solubilization at low ionic strength, ion-exchange chromatography, and gel filtration. The last indicated the Mr to be 370,000. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the pure enzyme...
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| Udgivet i: | J Bacteriol |
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| Principais autores: | , |
| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
American Society for Microbiology (ASM)
1986
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| Fag: | |
| Online adgang: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC214397/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/2867087/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.165.1.252-257.1986 |
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