HB GODAVARI [ALPHA-95(G2)PRO-]THR] - A NEUTRAL AMINO-ACID SUBSTITUTION IN THE ALPHA-1-BETA-2 INTERFACE THAT MODIFIES THE ELECTROPHORETIC MOBILITY OF HEMOGLOBIN

Hb Godavari [alpha 95(G2)Pro-->Thr] was characterized independently in two families of different ethnic origin. The first case, found in the Netherlands, involved an Indian patient. The second one was identifie d a few months later in an African family from Mall, living in France. Hb Godavari is the fourth example of a substitution involving neutral residues at position alpha 95(G2). In all these variants the electrop horetic pattern suggested that the structural modification unmasks a c harged residue buried in the alpha 1 beta 2 contact area. The oxygen a ffinity of this abnormal hemoglobin was approximately 10% higher than that of Hb A; in the absence of 2,3-diphosphoglycerate, its cooperativ ity was moderately decreased, suggesting a slightly unstable T state.