Two glutathioneS-transferase (GST) isozymes, GST-rl1 and GST-rl2, were purified from rabbit lenses and their properties were compared with those of other animals. GST-rl1 and GST-rl2 are dimeric enzymes whose subunit sizes are 24,000 and 21,500, respectively. The substrate specificities and inhibitor sensitivities of GST-rl1 and GST-rl2 are different from each other and from those of the isozymes from other animals. GST-rl1 immunologically crossreacted with the antibody against classμGST (rat GST Yb1-Yb1), and GST-rl2 crossreacted with the antibody against classπGST (rat GST Yp-Yp). N-Terminal amino acid sequences of GST-rl1 and GST-rl2 have great homology with other classμand classπenzymes, and thus indicate that they belong to classμand classπ, respectively. ClassπGST-rl2 is inactivated by 1,2-naphthoquinone, an oxidized metabolite of naphthalene, but classμGST-rl1 is insensitive to it. These results are similar to those of classπpig lens GST and classμbovine lens GST. Thus, the expression pattern of GST isozymes in lens varies with animal species, and may relate to their variation in sensitivity to oxidative stress.