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Staphylococcus aureus Growth using Human Hemoglobin as an Iron Source
Published on: February 7, 2013
Gel filtration of dilute human embryonic hemoglobins reveals basis for their increased oxygen binding
Lois R Manning1, Anthony M Popowicz2, Julio C Padovan3
1Department of Biology, Northeastern University, Boston, MA 02115, USA.
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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