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The binding of reduced nicotinamide adenine dinucleotide to citrate synthase of Escherichia coli K12

Biochemistry

Jan 13, 1976

Harry W Duckworth, E K Tong

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Abstract

Citrate synthase from Escherichia coli enhances the fluorescence of its allosteric inhibitor, NADH, and shifts the peak of emission of the coenzyme from 457 to 428 nm. These effects have been used to measure the binding of NADH to this enzyme under various conditions. The dissociation c...read more

Mentioned in this Paper

Fluorescence Spectroscopy
NADH
Hydrogen-Ion Concentration
Plasma Protein Binding Capacity
Macromolecular Compounds
Citrate (si)-Synthase
Oxo-Acid-Lyases
Alkalescens-Dispar Group
Paper Details
References
    • References11
    • Citations10
    • References11
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  • The binding of reduced nicotinamide adenine dinucleotide to citrate synthase of Escherichia coli K12

    Biochemistry

    Jan 13, 1976

    Harry W Duckworth, E K Tong

    PMID: 2277

    DOI: 10.1021/bi00646a017

    Abstract

    Citrate synthase from Escherichia coli enhances the fluorescence of its allosteric inhibitor, NADH, and shifts the peak of emission of the coenzyme from 457 to 428 nm. These effects have been used to measure the binding of NADH to this enzyme under various conditions. The dissociation c...read more

    Mentioned in this Paper

    Fluorescence Spectroscopy
    NADH
    Hydrogen-Ion Concentration
    Plasma Protein Binding Capacity
    Macromolecular Compounds

    Related Papers

    Paper Details
    References
    • References11
    • Citations10
    • References11
    • Citations10
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