Oxygen equilibrium and kinetics of isolated subunits from hemoglobin Kansas.

Abstract:

: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.

authors

Riggs A,Gibson QH

doi

10.1073/pnas.70.6.1718

subject

Has Abstract

pub_date

1973-06-01 00:00:00

pages

1718-20

issue

6

eissn

0027-8424

issn

1091-6490

journal_volume

70

pub_type

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