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Hemoglobin
international journal for hemoglobin research
Volume 5, 1981 - Issue 7-8
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Original Article

Hemoglobin Cubujuqui (α141 ARG-SER): Functional Consequences of the Alteration of the C-Terminus of the αChain of Hemoglobin

, , &
Pages 715-724 | Received 08 Jul 1981, Accepted 27 Aug 1981, Published online: 07 Jul 2009
 

Abstract

Hemoglobin Cubujuqui (1) was detected in several members of a Mexican-American family. Structural analysis of this hemoglobin indicated that the carboxyl terminal arginine at position 141 in the α chain had been replaced by serine. This residue is critical not only in stabilizing the deoxy or T conformation by electrostatic interactions, but it is also involved in the Bohr effect through its linkage with Val lα of the opposite a chain in the tetramer. The variant exhibits high affinity for oxygen that is associated with destabilization of the deoxy conformation, and reduced cooperativlty. The pH and the chloride sensitivity of the variant are also reduced, as compared to Hb A.

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