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Electrophoresis in a sucrose gradient at pH values between 5 and 8 separated housefly DDT [1,1,1-trichloro-2,2-bis-(p-chlorophenyl)ethane] dehydrochlorinase into two major fractions. GSH S-aryltransferase under similar conditions migrated as a single peak of activity. Separation of housefly homogenates or partially purified enzyme preparations by electrofocusing in a natural pH gradient also showed the presence of multiple forms of DDT dehydrochlorinase.

biochemical journal. cellular aspects

The separation of multiple forms of housefly 1,1,1-trichloro-2,2-bis-(<i>p</i>-chlorophenyl)-ethane (DDT) dehydrochlorinase from glutathione <i>S</i>-aryltransferase by electrofocusing and electrophoresis

The separation of multiple forms of housefly 1,1,1-trichloro-2,2-bis-(p-chlorophenyl)-ethane (DDT) dehydrochlorinase from glutathione S-aryltransferase by electrofocusing and electrophoresis