Electrophoretic and Stability Studies on Glutathione S-Aryltransferase and DDT Dehydrochlorinase

Abstract

1. Low voltage electrophoresis on cellulose acetate paper, high voltage paper electrophoresis, and density gradient electrophoresis have been applied to glutathione S-aryltransferase and DDT-dehydrochlorinase. 2. Density gradient electrophoresis was found to be excellent for enzyme separations. 3. Glutathione S-aryltransferase has been shown to be a distinct enzyme from DDT-dehydrochlorinase in the housefly, Musca domestica. 4. Both male and female houseflies appear to possess two distinct DDT-dehydrochlorinases. 5. Isoelectric points have been found for grass grub (Costelytra zealandica) and housefly glutathione S-aryltransferases and for both housefly DDT-dehydrochlorinases. 6. Electrophoretic mobilities have been calculated for housefly glutathione S-aryltransferase and DDT-dehydrochlorinases. 7 .pH stability curves have been plotted for the fly enzymes. 8. The molecular weights of the fly enzymes have been determined by gel filtration.