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Yeast glutathione reductase. Studies of the kinetics and stability of the enzyme as a function of pH and salt concentration

Biochimica Et Biophysica Acta

Nov 20, 1975

Gary Moroff, K G Brandt

PMID: 74

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Abstract

1. The pH dependencies of the apparent Michaelis constant for oxidized glutathione and the apparent turnover number of yeast glutathione reductase (EC 1.6.4.2) have been determined at a fixed concentration of 0.1 mM NADPH in the range pH 4.5--8.0. Between pH 5.5 and 7.6, both of these p...read more

Mentioned in this Paper

Glutathione Reductase
Study
Glutathione Disulfide
Drug Stability
Oxidation-Reduction
NADP
Sodium Acetate
Serum
Metabolic Inhibition
Enzyme Activation
1
2
Paper Details
References
    • References5
    • Citations10
    • References5
    • Citations10
  • Yeast glutathione reductase. Studies of the kinetics and stability of the enzyme as a function of pH and salt concentration

    Biochimica Et Biophysica Acta

    Nov 20, 1975

    Gary Moroff, K G Brandt

    PMID: 74

    DOI:

    Abstract

    1. The pH dependencies of the apparent Michaelis constant for oxidized glutathione and the apparent turnover number of yeast glutathione reductase (EC 1.6.4.2) have been determined at a fixed concentration of 0.1 mM NADPH in the range pH 4.5--8.0. Between pH 5.5 and 7.6, both of these p...read more

    Mentioned in this Paper

    Glutathione Reductase
    Study
    Glutathione Disulfide
    Drug Stability
    Oxidation-Reduction
    1
    2

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    Paper Details
    References
    • References5
    • Citations10
    • References5
    • Citations10
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