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The isolated beta subunit of hemoglobin Kansas has an oxygen affinity that is as low relative to the oxygen affinity of the beta(A) 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 beta(Kansas) (k = 37 sec(-1) and 18 sec(-1) for beta(Kansas) and beta(A), respectively) and from a lower association reaction rate, The properties of the alpha chains from hemoglobins A and Kansas appear to be identical, as expected.

Oxygen Equilibrium and Kinetics of Isolated Subunits from Hemoglobin Kansas