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Related Experiment Videos

Ligand kinetics in hemoglobin Hiroshima.

R L Nagel, Q H Gibson, H B Hamilton

    The Journal of Clinical Investigation
    |August 1, 1971
    PubMed
    Summary
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    Hemoglobin Hiroshima, a variant with increased oxygen affinity, exhibits faster ligand combination and slower dissociation rates. This kinetic profile explains its high oxygen-binding capacity and altered Bohr effect.

    Area of Science:

    • Biochemistry
    • Hematology
    • Molecular Biology

    Background:

    • Hemoglobin variants can exhibit altered oxygen-binding properties.
    • Hemoglobin Hiroshima is known for its high oxygen affinity and decreased Bohr effect.

    Purpose of the Study:

    • To elucidate the kinetic basis for the high oxygen affinity of Hemoglobin Hiroshima.
    • To understand the molecular mechanisms underlying altered ligand binding in this hemoglobin variant.

    Main Methods:

    • Electrophoretic analysis to characterize Hemoglobin Hiroshima.
    • Kinetic studies measuring oxygen and carbon monoxide binding and dissociation rates.
    • Dithionite-induced oxygen dissociation experiments.

    Main Results:

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    • Hemoglobin Hiroshima demonstrated an electrophoretically fast-moving pattern.
    • A fourfold increase in oxygen affinity was observed compared to normal hemoglobin.
    • The dissociation rate of O(2) in the presence of dithionite was decreased.
    • The binding rate of CO by the deoxy form was increased.

    Conclusions:

    • The high affinity of Hemoglobin Hiroshima is attributed to a combination of faster ligand association and slower ligand dissociation rates.
    • These kinetic alterations in ligand binding are the primary determinants of the variant's functional characteristics.