Acidic and basic forms of glutathione S-transferases from human placenta and comparison with human kidney glutathione S-transferase.
Glutathione S-transferase (GSH-transferase) was purified from human placenta and kidney by affinity chromatography on S-glutathione-carbamidomethyl-epsilon-aminolysyl-Sepharose CL 4B and gel filtration chromatography on Sephades G-75. Electrophoretically pure enzyme with the specific activities of 50.7 and 55.9 U/mg, respectively, were obtained. In addition to the known acidic isoenzyme from human placenta (isoelectric point, pI, 4.5), we describe here for the first time the presence of 6 basic forms with pI values between 8.0 and 9.0. The kidney GSH-transferase contained 2 acidic forms with isoelectric points at 4.6 and 4.65, and 6 basic forms with pI values between 8.7 and 9.4. The basic and acidic isoenzymes from placenta were separated by ion exchange chromatography on Sephadex DEAE A-25. The acidic form accounted for 36% of the total GSH-transferase activity from placenta. Antibodies against the kidney enzyme were raised in rabbit. Total cross-reactivity of placental GSH-transferase with antikidney-GSH-transferase antibodies was obtained, suggesting that the kidney and placental enzymes are immunologically closely related.
Steisslinger
H W
HW
Institut für Organische Chemie, Biochemie und Isotopenforschung, Universität, Stuttgart, BRD.
Pfleiderer
G
G
D000328:Adult; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D005982:Glutathione Transferase / Q000032:analysis*; D006801:Humans; D007526:Isoelectric Point; D007527:Isoenzymes / Q000032:analysis*; D007668:Kidney / Q000201:enzymology*; D010920:Placenta / Q000201:enzymology*
D007527:Isoenzymes; D005982:Glutathione Transferase