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.
journal_name
Proc Natl Acad Sci U S Aauthors
Riggs A,Gibson QHdoi
10.1073/pnas.70.6.1718subject
Has Abstractpub_date
1973-06-01 00:00:00pages
1718-20issue
6eissn
0027-8424issn
1091-6490journal_volume
70pub_type
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