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Subunit interactions in yeast glyceraldehyde-3-phosphate dehydrogenase

Biochemistry

Dec 16, 1975

S C MockrinDoug Koshland

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Abstract

The spontaneous inactivation of yeast glyceraldehyde-3-phosphate dehydrogenase was found to fit a simple two-state model at pH 8.5 and 25 degrees. The first step is a relatively rapid dissociation of the tetramer to dimers with the equilibrium largely in favor of the tetramer. In the ab...read more

Mentioned in this Paper

Inactivation
Nucleic Acid Hybridization Procedure
Glyceraldehyde-3-phosphate dehydrogenase
Ligands
Striadyne
NADH
Salts
Covalent Interaction
Protein Conformation
Sulfhydryl Compounds
49
1
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  • Subunit interactions in yeast glyceraldehyde-3-phosphate dehydrogenase

    Biochemistry

    Dec 16, 1975

    S C MockrinDoug Koshland

    PMID: 55

    DOI: 10.1021/bi00696a008

    Abstract

    The spontaneous inactivation of yeast glyceraldehyde-3-phosphate dehydrogenase was found to fit a simple two-state model at pH 8.5 and 25 degrees. The first step is a relatively rapid dissociation of the tetramer to dimers with the equilibrium largely in favor of the tetramer. In the ab...read more

    Mentioned in this Paper

    Inactivation
    Nucleic Acid Hybridization Procedure
    Glyceraldehyde-3-phosphate dehydrogenase
    Ligands
    Striadyne
    49
    1

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