Melgar Riol M J, Nóvoa Valiñas M C, García Fernández M A, Pérez López M
Department of Toxicology, Faculty of Veterinary Medicine, University of Santiago de Compostela, Avda. de Madrid s/n, 27002 Lugo, Spain.
Comp Biochem Physiol C Toxicol Pharmacol. 2001 Feb;128(2):227-35. doi: 10.1016/s1532-0456(00)00196-4.
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.
