Purification of a glutathione S-transferase that mediates fosfomycin resistance in bacteria.

The enzyme that modifies fosfomycin by formation of an adduct with glutathione was purified 12-fold with a 56% activity yield by passage through DEAE Sephacel and high-performance liquid chromatography molecular exclusion columns. Its functional form was a homodimer of two 16,000-dalton polypeptides...

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Опубліковано в::	Antimicrob Agents Chemother
Автори:	Arca, P, Hardisson, C, Suárez, J E
Формат:	Artigo
Мова:	Inglês
Опубліковано:	American Society for Microbiology (ASM) 1990
Предмети:	Research Article
Онлайн доступ:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC171703/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/2193621/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/aac.34.5.844
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