Purification and properties of housefly glutathione S-transferase

摘要: Abstract Glutathione S- transferases were partially purified from an insecticide resistant and a susceptible strain of houseflies characterized using 3,4-dichloronitrobenzene (DCNB) as the substrate. The molecular weight enzyme was estimated to be 50,000 SDS gel electrophoresis revealed that consisted two equal subunits 23,000. An Arrhenius plot temperature versus DCNB conjugation showed discontinuity at about 35°C. optimum pH for activity 9.5 10. A difference in equilibrium constants between enzymes strains did not explain higher overall reactions strain. same active methyl iodide conjugation, degradation organophosphorus insecticides γ-BHC, but inactive DDT-dehydrochlorination. via alkyl and/or “leaving group” conjugation.