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• W2012170730 abstract "Glutathione S-transferases (GST) form an important family of biotransformation enzymes catalyzing the conjugation of glutathione to a great variety of xenobiotic compounds. The objective of this study was to compare the different characteristics of GST from freshly isolated rainbow trout hepatocytes with those corresponding to the total liver of the same fish, in order to establish the similarities. GST was purified by affinity chromatography and enzymatic activity was determined towards two substrates, 1-chloro-2,4-dinitrobenzene (CDNB) and ethacrynic acid (ETHA). The different isoenzymes were determined by HPLC associated with SDS-PAGE. Slight differences between the samples were obtained when the results corresponding to the enzyme activity were compared. HPLC results showed that all GST isoforms present in the total liver samples were represented in the isolated cells too, corresponding to isoforms with molecular masses of approximately 25.5 and 23.0 kDa." @default.
• W2012170730 created "2016-06-24" @default.
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• W2012170730 date "2001-02-01" @default.
• W2012170730 modified "2023-09-30" @default.
• W2012170730 title "Glutathione S-transferases from rainbow trout liver and freshly isolated hepatocytes: purification and characterization" @default.
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• W2012170730 doi "https://doi.org/10.1016/s1532-0456(00)00196-4" @default.
• W2012170730 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11239835" @default.
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