Glutathione transferases in aquatic and terrestrial animals from nine phyla.

Glutathione transferase (GST) was present in 71 of 72 animal species/stages representing nine phyla when measured with 1-chloro-2,4-dinitrobenzene (CDNB). Our hypothesis that all animals have GST was not falsified. Transferase activity towards ethacrynic acid (ETHA) was present in species from all phyla investigated, but some animals seem to be without this activity. Activity towards 1,2-dichloro-4-nitrobenzene (DCNB) was less developed in aquatic animals than in terrestrial ones. The amount of protein binding to GSH-affinity gel matrix was rather uniform, ranging between 0.3 and 0.7% of soluble protein in homogenates of widely diverse animal species, thus being less variable than the enzyme activity. Transferases active towards DCNB did not bind at all or were less firmly bound to the GSH-affinity gel than the activity towards CDNB or ETHA. Fractionation was obtained by using a gradient of GSH. With SDS-electrophoresis it was demonstrated that the proteins with affinity to GSH had monomers in the MW-range 21.500-29.000. Hydra attenuata had one band (MW = 25,000); all other sources gave a complex pattern with up to six bands. It is concluded that GSTs are characteristic major constituents of animal cells, probably with some common basic function. Mutant forms able to aid detoxication are retained in the phylogenesis when they increase the fitness of the animal.