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. 1973 Jun;70(6):1718–1720. doi: 10.1073/pnas.70.6.1718

Oxygen Equilibrium and Kinetics of Isolated Subunits from Hemoglobin Kansas

Austen Riggs 1,2, Quentin H Gibson 1,2
PMCID: PMC433580  PMID: 4515930

Abstract

The isolated β subunit of hemoglobin Kansas has an oxygen affinity that is as low relative to the oxygen affinity of the βA subunit as the affinity of hemoglobin Kansas is low relative to hemoglobin A. Thus the low affinity properties of hemoglobin Kansas are almost completely reflected in the properties of the isolated subunits. The kinetic results show that the equilibrium affinity difference results both from a much larger oxygen dissocation rate constant in βKansas (k = 37 sec-1 and 18 sec-1 for βKansas and βA, respectively) and from a lower association reaction rate, The properties of the α chains from hemoglobins A and Kansas appear to be identical, as expected.

Keywords: hemoglobin A, β chains

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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