Abstract
Glutathione transferase was purified from Mucor javanicus and characterized as a dimer of identical subunits (Mr; 22, 000). Kinetics and Km values of M. javanicus glutathione transferase, 0.48 mM and 1.0 mM (at pH 6.5) for glutathione and 1-chloro-2, 4-dinitrobenzene, are close to those of rat liver enzyme, but occurrence of isoenzymes was not recognized in M. javanicus. The best substrate of M. javanicus glutathione transferase was 1-chloro-2, 4-dinitrobenzene. On the other hand, 2, 3-, 2, 4-, 2, 5-, and 3, 4-dichloronitrobenzenes were converted to the related conjugates by 0.17 to 0.35% of the velocity toward the best substrate. This is correlated to the previous result that 2, 3-and 2, 4-dichloronitrobenzenes were metabolized to 2-methylthio derivatives by the incubation with M. javanicus.
