Results 291 to 300 of about 428,300 (333)
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Glutathione Transferase: New Model for Glutathione Activation
Chemistry – A European Journal, 2008AbstractGlutathione transferases are enzymes of the cellular detoxification system that metabolize a vast spectrum of xenobiotic and endobiotic toxic compounds. They are homodimers or heterodimers and each monomer has an active center composed of a G‐site in which glutathione (GSH) binds and an H‐site for the electrophilic substrate.
Daniel F A R, Dourado +3 more
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Biochimica et Biophysica Acta, 1979
M. Moron, J. Depierre, B. Mannervik
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M. Moron, J. Depierre, B. Mannervik
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Detoxication reactions of glutathione and glutathione transferases
Xenobiotica, 1986(1986). Detoxication reactions of glutathione and glutathione transferases. Xenobiotica: Vol. 16, No. 10-11, pp. 957-973.
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Critical reviews in biochemistry and molecular biology, 1995
J. Hayes, D. Pulford
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J. Hayes, D. Pulford
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Glutathione transferases: Nomenclature
Biochemical Pharmacology, 1984W B, Jakoby, B, Ketterer, B, Mannervik
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Microsomal Glutathione Transferase 1
2005Microsomal glutathione transferase 1 (MGST1) is an abundant membrane-bound glutathione transferase and peroxidase constituting 3% of the endoplasmic reticulum protein in rat liver (and 5% of the outer mitochondrial membrane). The enzyme is most well studied in mammals and belongs to a large and widely distributed superfamily.
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