Phenoxyacetic acid induces glutathione-dependent detoxification and depletes the glutathione pool in Penicillium chrysogenum
✍ Scribed by Tamás Emri; Dr. István Pócsi; Attila Szentirmai
- Publisher
- John Wiley and Sons
- Year
- 1997
- Tongue
- English
- Weight
- 370 KB
- Volume
- 37
- Category
- Article
- ISSN
- 0233-111X
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✦ Synopsis
Enzymes of the glutathione-dependent detoxification pathway (glutathione S-transferase and y-glutamyltranspeptidase) I) were induced, and the glutathione pool was completely depleted by phenoxyacetic acid in Penicillium chrysogenum mycelia incubated for 15 h in a culture medium containing lactose as a carbon source and sodium glutamate as a nitrogen source. A significant increase in both the oxidised glutathione concentrations and the glutathione reductase activities were also observed. 1 -Chloro-2,4-dinitrobenzene -a potent substrate and inducer of glutathione S-transferaseinitiated very similar physiological changes but no /3-lactam production could be detected in this case. When (NH4),HPO4 was used as a nitrogen source the penicillin biosynthesis was repressed and the induction of y-glutamyltranspeptidase by phenoxyacetic acid was hindered considerably.
📜 SIMILAR VOLUMES
## Abstract The glutathione (GSH) S‐conjugation of 1,2‐epoxy‐3‐(4′‐nitrophenoxy)propane was catalysed predominantly by microsomal glutathione S‐transferase (mGST) in __Penicillium chrysogenum__. The specific mGST activity unlike the cytosolic GST (cGST) activity increased substantially when the pen