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Aggregation of deoxyhemoglobin subunits.

P McGovern, P Reisberg, J S Olson

    The Journal of Biological Chemistry
    |December 25, 1976
    PubMed
    Summary
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    This study reveals how deoxyhemoglobin chains aggregate, detailing reaction rates influenced by pH and chemical additions. Organic phosphates, like inositol hexaphosphate, impact hemoglobin formation by affecting beta chain tetramer dissociation and binding affinities.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Protein Chemistry

    Background:

    • Deoxyhemoglobin formation involves the aggregation of isolated alpha and beta globin chains.
    • Understanding these aggregation kinetics is crucial for comprehending hemoglobin assembly and function.

    Purpose of the Study:

    • To elucidate the kinetic mechanisms governing deoxyhemoglobin formation from isolated alpha and beta chains.
    • To investigate the influence of pH, heme concentration, and organic phosphates on chain aggregation rates.

    Main Methods:

    • Spectrophotometric measurement of heme spectral changes during alpha and beta chain aggregation.
    • Kinetic analysis of monomer and dimer aggregation reactions.
    • Assessment of the effects of p-hydroxymercuribenzoate and inositol hexaphosphate on aggregation rates.

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    Main Results:

    • At low heme concentrations, tetramer formation follows two consecutive second-order reactions.
    • pH variations uniformly decrease aggregation rates due to subunit charge repulsion.
    • Organic phosphates, particularly inositol hexaphosphate, modulate beta chain tetramer dissociation and binding affinities, influencing overall hemoglobin formation velocity.

    Conclusions:

    • Deoxyhemoglobin formation kinetics are complex, involving sequential monomer and dimer aggregation.
    • pH and specific chemical agents significantly alter these aggregation rates.
    • Inositol hexaphosphate plays a key role in regulating beta chain tetramer dissociation and exhibits concentration-dependent effects on hemoglobin assembly.