Abstract
Hb Calais [β 76 (E20) Ala → Pro] is a new human hemoglobin variant displaying a decreased oxygen affinity. The only electrophoretical difference with Hb A was a slight more acidic isoelectric point. A 2-fold decrease in the oxygen affinity was found by equilibrium measurements performed in a suspension of intact red blood cells and in the lysate. It was confirmed by kinetic studies of the purified abnormal hemoglobin. The rte of methamoglobin formation at 37°C of Hb Calais was also increased realtive to Hb A. The mechanism by which the Pro for Ala substitution of an external residue in the β-chains results in these profound functional abnormalities is nuclear. Subtle changes at the heme pocket, at a distance from teh mutation, may be a plausible explanation for the effects observed.
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