Equilibrium and kinetic constants for the thiol-disulfide interchange reaction between glutathione and dithiothreitol.
AUTOR(ES)
Rothwarf, D M
RESUMO
The equilibrium and rate constants for the reaction between oxidized and reduced glutathione and oxidized and reduced dithiothreitol have been determined at several pH values and temperatures. The measurements involve approach to equilibrium from both directions, quenching of the reaction by lowering the pH or by addition of methyl methanethiosulfonate, separation of reactants and products by reverse-phase HPLC, and determination of their concentrations. Analysis of reaction mixtures was carried out at various times to assure that equilibrium had been reached and to determine kinetic constants prior to the attainment of equilibrium.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=49831Documentos Relacionados
- The relationship between thiol-disulfide balance and idiopathic sudden sensorineural hearing loss
- Changes in the glutathione thiol-disulfide status of Neurospora crassa conidia during germination and aging.
- Thiol-disulfide effects on hepatic glutathione transport. Studies in cultured rat hepatocytes and perfused livers.
- Inhibition of human immunodeficiency virus infection by agents that interfere with thiol-disulfide interchange upon virus-receptor interaction.
- Cloning and characterization of the gene for a protein thiol-disulfide oxidoreductase in Bacillus brevis.