TY - JOUR
T1 - Hemoglobin cubujuqui (α141 ARG-SER)
T2 - Functional consequences of the alteration of the c-terminus of the αchain of hemoglobin
AU - Moo-Penn, Winston F.
AU - Therrell, Bradford L.
AU - Jue, Danny L.
AU - Johnson, Mary H.
N1 - Copyright:
Copyright 2016 Elsevier B.V., All rights reserved.
PY - 1981
Y1 - 1981
N2 - 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Structural analysis of this hemoglobin indicated that the carboxyl terminal arginine at position 141 in the α chain had been replaced by serine.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.
AB - 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Structural analysis of this hemoglobin indicated that the carboxyl terminal arginine at position 141 in the α chain had been replaced by serine.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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U2 - 10.3109/03630268108991839
DO - 10.3109/03630268108991839
M3 - Article
C2 - 7338473
AN - SCOPUS:0019767773
VL - 5
SP - 715
EP - 724
JO - Hemoglobin
JF - Hemoglobin
SN - 0363-0269
IS - 7-8
ER -