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Abstract
A hemoglobin variant was identified as hemoglobin Mobile in which valine replaces the normal aspartic acid at β73. studies of its oxygen equilibria and of its interactions in gelation when mixed with hemoglobin S were carried out. Hemoglobin Mobile had an oxygen affinity lower than that of hemoglobin A, as observed by others. However, in mixtures with hemoglobin S, hemoglobin Mobile appeared to impair gelation or increase solubility to a slightly greater extent than did hemoglobin A. Beta73 is a known site of intermolecular interactions in polymers of hemoglobin S. Our studies suggest that the impairment of hemoglobin S polymer formation by altered intermolecular interactions is significantly less in Hb Mobile than in Hb Korle-Bu in which β73 is asparagine.