The comparative in vitro glutathione S-transferase activity in selected plants, fish, insects and mammalian species measured with four different second substrates

• Published in: Marine environmental research 1995, Vol.39 (1), p.350-351
• Main Authors: Egaas, E., Falls, J.G., Dauterman, W.C., Collier, T.K., Skaare, J.U.
• Format: Article
• Language: English
• ISSN: 0141-1136; 1879-0291
• DOI: 10.1016/0141-1136(95)98397-U

The glutathione S-transferases (GSTs) is a multigene family of enzymes whose isoforms exhibit differing but often overlapping substrate specificities for both endogenous and exogenous compounds. The major GSTs are soluble cytosolic proteins which conjugate glutathione to electrophilic centres of a wide range of exogenous compounds. The wide distribution of GSTs in living cells has been demonstrated with the use of 1-chloro-2,4-dinitrobenzene (CDNB), which is a very active substrate with most of the GSTs tested. Within recent years, it has become apparent that the in vivo production of GSTs is a process that may be markedly responsive to the action of endogenous and exogenous inducers. Because of this, GSTs have been suggested as possible bioindicators of pollution. The induction of GST activity may be due to the increased activity of specific isozymes with a certain substrate specificity specter. Thus, substrates more specific for certain isozymes than CDNB may be more sensitive in detection of apparent induction of GST. However, more comparative information is needed about the distribution and substrate specificities of GSTs in living organisms. The in vitro activity of GST in 1 plant, 3 fish, 2 insect and 2 mammalian species with ethacrynic acid, atrazine, 1,2-dichloro-4-nitrobenzene and CDNB is presented. The recoveries of the respective GST activities after partial purification of rainbow trout and mouse GST through a GSH-affinity Sepharose 6B is discussed.