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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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Detalhes bibliográficos
Publicado no:J Bacteriol
Principais autores: Leng, J, Cameron, A J, Buckel, S, Kennelly, P J
Formato: Artigo
Idioma:Inglês
Publicado em: American Society for Microbiology (ASM) 1995
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Acesso em linha: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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