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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| Publicado en: | Antimicrob Agents Chemother |
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| Autores principales: | , , |
| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
American Society for Microbiology (ASM)
1990
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| Materias: | |
| Acceso en línea: | 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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