Are the steady state kinetics of glutathione transferase always dependent on the deprotonation of the bound glutathione? New insights in the kinetic mechanism of GST P 1-1.
Caccuri, A M
Are the steady state kinetics of glutathione transferase always dependent on the deprotonation of the bound glutathione? New insights in the kinetic mechanism of GST P 1-1. [electronic resource] - Biochemical and biophysical research communications May 1994 - 1428-34 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0006-291X
10.1006/bbrc.1994.1610 doi
4-Chloro-7-nitrobenzofurazan--chemistry
Glutathione--metabolism
Glutathione Transferase--metabolism
Humans
Hydrogen-Ion Concentration
Kinetics
Oxidation-Reduction
Are the steady state kinetics of glutathione transferase always dependent on the deprotonation of the bound glutathione? New insights in the kinetic mechanism of GST P 1-1. [electronic resource] - Biochemical and biophysical research communications May 1994 - 1428-34 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0006-291X
10.1006/bbrc.1994.1610 doi
4-Chloro-7-nitrobenzofurazan--chemistry
Glutathione--metabolism
Glutathione Transferase--metabolism
Humans
Hydrogen-Ion Concentration
Kinetics
Oxidation-Reduction