Gel filtration of dilute human embryonic hemoglobins reveals basis for their increased oxygen binding

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 other...

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Published inAnalytical biochemistry Vol. 519; pp. 38 - 41
Main Authors Manning, Lois R., Popowicz, Anthony M., Padovan, Julio C., Chait, Brian T., Manning, James M.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 15.02.2017
Subjects
Allosteric Regulation
Chromatography, Gel - methods
Development
Embryo, Mammalian - metabolism
Gel filtration
Hemoglobin
Hemoglobins - chemistry
Hemoglobins - metabolism
Hemoglobins, Abnormal - chemistry
Hemoglobins, Abnormal - metabolism
Humans
Hydrogen-Ion Concentration
Kinetics
Oxygen - metabolism
Oxygen affinity
Protein Binding
Subunit assembly
Thermodynamics
Gel filtration
Hemoglobin
Development
Oxygen affinity
Subunit assembly
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Summary: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.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 23
ISSN:0003-2697
1096-0309
DOI:10.1016/j.ab.2016.12.008