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Primitive haemoglobin

B Tiplady, M Goodman

    Journal of Molecular Evolution
    |August 5, 1977
    PubMed
    Summary
    This summary is machine-generated.

    Comparing Petromyzon and Aplysia globins reveals conserved interior positions in mollusc-vertebrate evolution. Lamprey hemoglobin

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    Area of Science:

    • Evolutionary biology
    • Molecular evolution
    • Biochemistry

    Background:

    • Globin sequences provide insights into evolutionary processes.
    • Understanding residue position evolution is key to deciphering molecular changes.
    • Comparative analysis of diverse species aids in reconstructing ancestral states.

    Purpose of the Study:

    • To compare Petromyzon (lamprey) and Aplysia (sea hare) globin sequences.
    • To investigate evolutionary rates across different residue positions.
    • To infer ancestral globin characteristics and evolutionary patterns.

    Main Methods:

    • Sequence alignment of Petromyzon and Aplysia globins.
    • Comparison with postulated vertebrate and mollusc-vertebrate ancestral sequences.

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  • Analysis of residue conservation patterns at various positions.

    • Main Results:

    • Interior residue positions show relative conservation between the mollusc-vertebrate ancestor and Aplysia globin.
    • The alpha 1 beta 2 contact area in Petromyzon haemoglobin evolution is notably conserved.
    • Homopolymeric binding in lamprey hemoglobin suggests a primitive functional trait.

    Conclusions:

    • Evolutionary rates vary across globin residue positions.
    • Specific regions like interior positions and contact areas exhibit conserved evolutionary trajectories.
    • Lamprey hemoglobin's binding mechanism may represent an ancestral characteristic.