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This research investigates how the composition of a redox buffer affects the rate of oxidative renaturation of ribonuclease A catalyzed by protein disulfide isomerase.

January 1, 1991Biochemistry

Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer

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MLMichelle LylesMarlboro College HGHiram GilbertBaylor College of Medicine

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Randomized trial shows the dependence of oxidative folding rate on redox buffer composition, indicating optimal glutathione levels.

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This research investigates how the composition of a redox buffer affects the rate of oxidative renaturation of ribonuclease A catalyzed by protein disulfide isomerase.
Analyzed the effect of varying concentrations of glutathione and glutathione disulfide on the velocity of oxidative folding.
Measured the apparent kcat for the PDI-catalyzed reaction at specific glutathione concentrations.
Optimum activity occurs at [GSH] = 1.0 mM and [GSSG] = 0.2 mM.
The kcat for the PDI-catalyzed reaction is 0.46 +/- 0.05 mumol of RNase renatured min-1 (mumol of PDI)-1.
The rate of the catalyzed reaction increases as the ratio [GSH]2/[GSSG] exceeds 1 mM, with the maximum rate acceleration observed under sufficiently reducing conditions.

Cite This Study

Lyles et al. (1991) studied this question.

synapsesocial.com/papers/6a75956be244091301600331 https://doi.org/10.1021/bi00217a004

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Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer

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Cite This Study

Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer

Discussion

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Implication

Key Points

Cite This Study

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