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Abstract
We prepared six recombinant hemoglobin A variants [rHb(X)], in which Lys-α99 residues are replaced with different amino acids. The mutations with neutral amino acids decreased the O2 affinity and increased the dissociation constant of the Hb tetramer (α2β2) to two αβ dimers. In particular, rHb(Lys-α99→Ala) showed the moderately low O2 affinity, which was insensitive to chloride anion concentration. The Ala mutant could be a promising material for artificial O2 carrier as red blood cell substitute.
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