Abstract
SummarySeven abnormal hemoglobins were investigated for an effect on the gelation of Hb S in the deoxy- or oxy-conformation. A positive effect (decreased MGC) was associated with substitution of Glu β6, Glu β26 and Glu β121. No difference was observed between the deoxy- or oxy-hemoglobins except in the case of Hb N-Baltimore which, in the deoxy state, exhibits a strongly negative effect on gelation but behaves like Hb A in the oxy state.
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