Steady-state kinetic studies of glutathione reductase |
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Authors: | M T Serafini A Romeu |
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Affiliation: | Departamento de Ingeniería Química y Bioquímica, Universidad de Barcelona, Tarragona, Spain. |
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Abstract: | The steady-state kinetic studies of yeast glutathione reductase, performed when [GSSG] = 10[NADPH] in the assay mixture, show that at concentrations of GSSG under 450 microM the enzymatic mechanism pathway is ping-pong. Furthermore, in the case of higher values, the enzymatic kinetics follows a sequential pathway. However when the glutathione reductase reaction passes to the ping-pong mechanism, the inhibition effect by excess of NADPH is stronger than when the reaction takes place over the sequential mechanism. |
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