Purification and some properties of glutathione S-transferase from Escherichia coli B.

Glutathione S-transferase was purified approximately 2,300-fold from cell extracts of Escherichia coli B with a 7.5% activity yield. The molecular weight of the enzyme was 45,000, and the enzyme appeared to consist of two homogeneous subunits. The enzyme was almost specific to 1-chloro-2,4-dinitrobe...

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Detalhes bibliográficos

Publicado no:	J Bacteriol
Principais autores:	Iizuka, M, Inoue, Y, Murata, K, Kimura, A
Formato:	Artigo
Idioma:	Inglês
Publicado em:	American Society for Microbiology (ASM) 1989
Assuntos:	Research Article
Acesso em linha:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC210469/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/2553668/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.171.11.6039-6042.1989
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