Explanation of the non-hyperbolic kinetics of the glutathione S-transferases by the simplest steady-state random sequential Bi Bi mechanism
- 1 June 1990
- journal article
- research article
- Published by Elsevier in Biochemical Pharmacology
- Vol. 39 (12) , 1999-2004
- https://doi.org/10.1016/0006-2952(90)90621-q
Abstract
No abstract availableThis publication has 18 references indexed in Scilit:
- Relaxed thiol substrate specificity of glutathione transferase effected by a non‐substrate glutathione derivativeFEBS Letters, 1988
- Glutathione Transferases—Structure and Catalytic ActivitCritical Reviews in Biochemistry, 1988
- Kinetic independence of the subunits of cytosolic glutathione transferase from the ratBiochemical Journal, 1985
- Structural, functional and hybridization studies of the glutathione S-transferases of rat liverBiochemical Pharmacology, 1983
- A nonlinear regression program for small computersAnalytical Biochemistry, 1981
- Multiple inhibition of glutathione S-transferase A from rat liver by glutathione derivatives: kinetic analysis supporting a steady-state random sequential mechanismBiochemical Journal, 1979
- A Steady‐State‐Kinetic Random Mechanism for Glutathione S‐Transferase A from Rat LiverEuropean Journal of Biochemistry, 1977
- Absence of a ping‐pong pathway in the kinetic mechanism of glutathione S‐transferase a from rat liver. Evidence based on quantitative comparison of the asymptotic properties of experimental data and alternative rate equationsFEBS Letters, 1975
- Purification and characterization of two glutathione S-aryltransferase activities from rat liver.Biochemical Journal, 1975
- Glutathione S-Transferase AJournal of Biological Chemistry, 1974