Article
Additive effects of beta chain mutations in low oxygen affinity hemoglobin betaF41Y,K66T.
The Journal of biological chemistry - 3 Sept 1999
Baudin-Creuza V, Vasseur-Godbillon C, Griffon N, Kister J, Kiger L, Poyart C, Marden M C, Pagnier J
Abstract excerpt
In order to decrease significantly the oxygen affinity of human hemoglobin, we have associated the mutation betaF41Y with another point mutation also known to decrease the oxygen affinity of Hb. We have synthesized a recombinant Hb (rHb) with two mutations in the beta chains: rHb betaF41Y,K66T. In the absence of 2, 3-diphosphoglycerate, additive effects of the mutations are evident, since the doubly mutated Hb...
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