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  • Title: Gel filtration of dilute human embryonic hemoglobins reveals basis for their increased oxygen binding.
    Author: Manning LR, Popowicz AM, Padovan JC, Chait BT, Manning JM.
    Journal: Anal Biochem; 2017 Feb 15; 519():38-41. PubMed ID: 27965062.
    Abstract:
    This report establishes a correlation between two known properties of the human embryonic hemoglobins-- their weak subunit assemblies as demonstrated here by gel filtration at very dilute protein concentrations and their high oxygen affinities and reduced cooperativities reported previously by others but without a mechanistic basis. We demonstrate here that their high oxygen affinities are a consequence of their weak assemblies. Weak vs strong hemoglobin tetramers represent a regulatory mechanism to modulate oxygen binding capacity by altering the equilibrium between the various steps in the assembly process that can be described as an inverse allosteric effect.
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