A human glutathione S-transferase isozyme designated as hGST 5.8 has b
een previously characterized in human liver (Singhal et al. Biochim. B
iophys. Acta 1204, 279-286, 1994). In the present studies, polyclonal
antibodies highly specific for hGST 5.8 were obtained by a two-step pr
ocedure. First, antibodies were raised against total human liver gluta
thione S-transferases obtained by glutathione affinity chromatography.
The total antibody pool was then successively immunoabsorbed with hum
an GSTs of the alpha, mu, and pi class antigens. The resulting polyclo
nal antibodies recognized only hGST 5.8 among human liver GSTs. While
these antibodies also recognized mouse GSTA4-4 and rat GST 8-8, sugges
ting a structural interrelationship among these enzymes, the recogniti
on was weaker than that of the human hGST 5.8. The pattern produced in
Ouchterlony double diffusion tests indicated the presence of epitopes
in the human enzyme that are absent from its rodent counterparts.