Purification and characterization of a labile rat glutathione transferase of the Mu class.
A labile GSH transferase homodimer termed 11-11 was purified from rat testis by GSH-agarose affinity chromatography followed by anion-exchange f.p.l.c. The enzyme is unstable in the absence of thiol(s) and has relatively low affinity for both 1-chloro-2,4-dinitrobenzene (Km 4.4 mM) and GSH (Km(app.) 4.4mM). Its mobility on SDS/polyacrylamide-gel electrophoresis is slightly less than that of subunits 3 and 4 and its pI is 5.2. Subunit 11 has a blocked N-terminal amino acid residue, but after CNBr cleavage fragments accounting for 113 amino acid residues were sequenced and showed 65% homology with corresponding sequences in subunit 4, indicating that it is a member of the Mu family. GSH transferase 11 is a major isoenzyme in testis, epididymis, prostate and brain and present at lower concentrations in other tissues.
Kispert
A
A
Department of Biochemistry, University College and Middlesex School of Medicine, London, U.K.
Meyer
D J
DJ
Lalor
E
E
Coles
B
B
Ketterer
B
B
D000818:Animals; D005982:Glutathione Transferase / Q000145:classification / Q000235:genetics / Q000302:isolation & purification*; D007527:Isoenzymes / Q000145:classification / Q000302:isolation & purification*; D005810:Multigene Family; D051381:Rats
D007527:Isoenzymes; D005982:Glutathione Transferase