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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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Sonraí Bibleagrafaíochta
Main Authors: Iizuka, M, Inoue, Y, Murata, K, Kimura, A
Formáid: Artigo
Teanga:Inglês
Foilsithe: 1989
Ábhair:
Rochtain Ar Líne:https://ncbi.nlm.nih.gov/pmc/articles/PMC210469/
https://ncbi.nlm.nih.gov/pubmed/2553668
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