PMID: 8937881Jan 1, 1996Paper

Metal-catalyzed oxidation and cleavage of octopus glutathione transferase by the Cu(II)-ascorbate system

Free Radical Biology & Medicine
S S TangG G Chang

Abstract

Glutathione transferase (GST) from octopus hepatopancreas was rapidly inactivated by micromolar concentration of Cu(II) in the presence of ascorbate at neutral pH and 0 degree C. Omitting the metal ion or ascorbate, or replacing the Cu(II) with Fe(II) did not result in any inactivation. Glutathione or the conjugation product of glutathione and 1-chloro-2,4-dinitrobenzene offered complete protection of the enzyme from Cu(II)-induced inactivation. 1-Chloro-2,4-dinitrobenzene, however, did not provide any protection. The inactivation was time and Cu(II) concentration dependent. The dependence of inactivation rate on Cu(II) concentration displayed saturation kinetics, which suggests that the inactivation occurs in two steps with Cu(II) binding with the enzyme first (KdCu = 260 microM), then the locally generated free radicals modify the essential amino acid residues in the active center, which results in enzyme inactivation. The Cu(II)-ascorbate system is, thus, an affinity reagent for the octopus GST. The enzyme inactivation was demonstrated to be followed by protein cleavage. Native octopus GST has a subunit M(r) of 24,000. The inactivated enzyme was cleaved at the C-terminal domain (domain II) of the enzyme molecule and resulted...Continue Reading

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Citations

Sep 6, 2000·Journal of Biomedical Science·T C ChangG G Chang
Feb 10, 2010·Journal of Biochemical and Molecular Toxicology·Alex J Salazar-MedinaRogerio R Sotelo-Mundo
Jan 19, 2019·Ecotoxicology and Environmental Safety·Rui CompanyAmparo Torreblanca
Apr 17, 2007·Comparative Biochemistry and Physiology. Toxicology & Pharmacology : CBP·I CunhaL Guilhermino

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