POLYCLONAL ANTIBODIES SPECIFIC TO HUMAN-GLUTATHIONE-S-TRANSFERASE-5.8(HGST-5.8)

Citation
Ss. Singhal et al., POLYCLONAL ANTIBODIES SPECIFIC TO HUMAN-GLUTATHIONE-S-TRANSFERASE-5.8(HGST-5.8), Biochemical archives, 11(4), 1995, pp. 189-195
Citations number
22
Categorie Soggetti
Biology
Journal title
ISSN journal
07495331
Volume
11
Issue
4
Year of publication
1995
Pages
189 - 195
Database
ISI
SICI code
0749-5331(1995)11:4<189:PASTH>2.0.ZU;2-#
Abstract
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.