Toxicology of Glutathione Transferases by Yogesh C. Awasthi

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By Yogesh C. Awasthi

Crucial enzymes keeping human and different organisms from in all probability poisonous chemical substances, Glutathione S-transferases (GSTs) are valuable to uncomplicated mechanisms resembling rigidity reaction and physiological services together with safety opposed to lipid peroxidation. This publication describes the position of GST in toxicology, targeting their pharmacologic and physiological roles and their relevance to organic toxicology. It covers constitution and serve as, gene rules, and those enzymes’ involvement in sign transduction. Reflecting present developments during this increasing learn zone, Toxicology of Glutathione Transferases is the single resource that info the equipment of GST examine.

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14, 3, 2005. 78. P. , The Anopheles gambiae detoxification chip: a highly specific microarray to study metabolic-based insecticide resistance in malaria vectors, Proc. Natl. Acad. Sci. USA 102, 4080, 2005. 79. Prapanthadara, L. , Isoenzymes of glutathione S-transferase from the mosquito Anopheles dirus species B: the purification, partial characterization, and interaction with various insecticides, Insect Biochem. Mol. Biol. 30, 395, 2000. 80. Sawicki, R. , Cloning, expression, and biochemical characterization of one Epsilon-class (GST-3) and ten Delta-class (GST-1) glutathione S-transferases from Drosophila melanogaster, and identification of additional nine members of the Epsilon class, Biochem.

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81. Ding, Y. , Characterization of the promoters of Epsilon glutathione transferases in the mosquito Anopheles gambiae and their response to oxidative stress, Biochem. J. 387, 879, 2005. 82. , The glutathione S-transferase D genes. A divergently organized, intronless gene family in Drosophila melanogaster, J. Biol. Chem. 268, 9737, 1993. 83. H. , Biochemical characterization of Drosophila glutathione S-transferases D1 and D21, J. Biol. Chem. 269, 27876, 1994. 84. C. , Drosophila glutathione S-transferase D27: functional analysis of two consecutive tyrosines near the N-terminus, Biochem.

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