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Some Properties of Hemoglobin Mobile (α2β273Asp→Val)

James L. Converse, Vijay Sharma, Gwen Reiss-Rosenberg, Helen M. Ranney, Elizabeth H. Danish, Lynda Bowman, John William Harris

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Abstract

A hemoglobin variant was identified as hemoglobin Mobile in which valine replaces the normal aspartic acid at beta 73. 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. Beta 73 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 beta 73 is asparagine.

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What this paper is about

A hemoglobin variant was identified as hemoglobin Mobile in which valine replaces the normal aspartic acid at beta 73. 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. Beta 73 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 beta 73 is asparagine.

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Available abstract

A hemoglobin variant was identified as hemoglobin Mobile in which valine replaces the normal aspartic acid at beta 73. 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. Beta 73 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 beta 73 is asparagine.

Key concepts: Hemoglobin, Chemistry, Biochemistry

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