Purification and characterization of an inorganic pyrophosphatase from the extreme thermophile Thermus aquaticus.
An inorganic pyrophosphatase was purified over 600-fold to homogeneity as judged by polyacrylamide gel electrophoresis. The enzyme is a tetramer of Mr = 84,000, has a sedimentation coefficient of 5.8S, a Stokes radius of 3.5 nm, and an isoelectric point of 5.7. Like the enzyme of Escherichia coli, t...
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| Pubblicato in: | J Bacteriol |
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| Autori principali: | , , , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
American Society for Microbiology (ASM)
1986
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC213453/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/3020000/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.168.1.318-321.1986 |
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