Purification and characterization of a major glutathione S-transferase from the mosquito Anopheles dirus (Species B)

The major form of glutathione S-transferase (GST) activity from the mosquito Anopheles dirus (species B), a vector of malaria in Thailand has been purified 421-fold. It constituted approx. 20% of the total measured CDNB conjugating activity in the homogenate. This enzyme appeared as a single band of...

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Veröffentlicht in:	Insect biochemistry and molecular biology 1996-03, Vol.26 (3), p.277-285
Hauptverfasser:	Prapanthadara, La-Aied, Koottathep, Surangchit, Promtet, Nongkran, Hemingway, Janet, Ketterman, Albert J.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Anopheles - enzymology Anopheles dirus Culicidae DDT (pesticide) ddt-dehydrochlorinase Diptera enzyme activity enzyme inhibitors Enzyme Inhibitors - pharmacology Glutathione glutathione transferase Glutathione Transferase - chemistry Glutathione Transferase - isolation & purification GST inhibition insecticide resistance Kinetics Molecular Sequence Data Mosquito purification S-transferase Substrate Specificity
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