Isolation and cloning of a protein-serine/threonine phosphatase from an archaeon.
A divalent metal ion-stimulated protein-serine/threonine phosphatase, PP1-arch, was purified approximately 1,000-fold from the extreme acidothermophilic archaeon Sulfolobus solfataricus (ATCC 35091). Purified preparations contained 40 to 70% of total protein as PP1-arch, as determined by assay-ing s...
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| Опубліковано в:: | J Bacteriol |
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| Автори: | , , , |
| Формат: | Artigo |
| Мова: | Inglês |
| Опубліковано: |
American Society for Microbiology (ASM)
1995
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| Предмети: | |
| Онлайн доступ: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC177503/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/7592428/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.177.22.6510-6517.1995 |
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