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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Bibliografiske detaljer

Udgivet i:	J Bacteriol
Principais autores:	Leng, J, Cameron, A J, Buckel, S, Kennelly, P J
Format:	Artigo
Sprog:	Inglês
Udgivet:	American Society for Microbiology (ASM) 1995
Fag:	Research Article
Online adgang:	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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