Hemoglobin Yakina. I. Clinical and biochemical studies.
Three members of a family who have erythrocytosis and a new hemoglobin, designated hemoglobin Yakima, are described. The abnormal hemoglobin is characterized by the substitution of histidine for aspartic acid at residue 99 in the beta-chain. Of three possible structure-function relations which would account for the increased oxygen affinity of hemoglobin Yakima, only two seem likely. These are: (a) an intrachain shift in the normal relations between the F and G helices and the heme group, or (b) an effect of the substituted side chain at a region of contact between nonpolar residues of the alpha- and beta-chains which favors the oxyhemoglobin quarternary structure.
D001224:Aspartic Acid; D005260:Female; D006455:Hemoglobins, Abnormal / Q000032:analysis*; D006639:Histidine; D006801:Humans; D011086:Polycythemia / Q000235:genetics*
D006455:Hemoglobins, Abnormal; D001224:Aspartic Acid; D006639:Histidine