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Related Experiment Videos

A polymerising Root-effect fish hemoglobin with high subunit heterogeneity. Correlation with primary structure

A Fago1, M Romano, M Tamburrini

  • 1Institute of Protein Biochemistry and Enzymology, Consiglio Nazionale delle Ricerche, Naples, Italy.

European Journal of Biochemistry
|December 15, 1993
PubMed
Summary
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The teleost fish Chelodonichthys kumu has a unique hemoglobin with functional heterogeneity between its alpha and beta chains, impacting oxygen binding. This functional difference, possibly due to an Ile substitution, is key to understanding its low cooperativity.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Fish Physiology

Background:

  • Teleost fish possess a single hemoglobin type.
  • Chelodonichthys kumu hemoglobin exhibits unique structural and functional properties.

Purpose of the Study:

  • To elucidate the complete amino acid sequence of the alpha and beta chains of C. kumu hemoglobin.
  • To investigate the functional heterogeneity and low cooperativity of this hemoglobin.
  • To determine the role of specific amino acid substitutions and allosteric effectors on hemoglobin function.

Main Methods:

  • Amino acid sequencing of alpha and beta chains.
  • Kinetic experiments on oxygen and carbon monoxide binding/dissociation.
  • Analysis of pH-dependent functional heterogeneity.

Related Experiment Videos

  • Investigation of allosteric effector (ATP) effects.

    • Main Results:

    • The complete amino acid sequence of C. kumu hemoglobin chains was established.
    • A reactive cysteine residue leads to beta-chain polymerization via disulfide bridges without functional alteration.
    • Significant pH-dependent functional heterogeneity between alpha and beta chains was observed, reducing cooperativity.
    • ATP stabilizes the T state at lower pH, influencing quaternary equilibrium.
    • An Ile substitution at position E11 may cause subunit functional heterogeneity, particularly affecting oxygen access to the beta chain.

    Conclusions:

    • C. kumu hemoglobin displays functional heterogeneity and low cooperativity, primarily driven by pH-dependent differences in chain kinetics.
    • The E11 Ile substitution is a likely contributor to the observed subunit functional heterogeneity.
    • ATP modulates hemoglobin function by stabilizing the T state rather than enhancing heterogeneity.