Hemoglobin Yakina. I. Clinical and biochemical studies.

Abstract

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.

• Authors: R T Jones, E E Osgood, B Brimhall, R D Koler
• Journal: The Journal of clinical investigation (J Clin Invest) Vol. 46 Issue 11 Pg. 1840-7 (Nov 1967) ISSN: 0021-9738 [Print] United States
• PMID: 6061751 (Publication Type: Journal Article)

Chemical References

• Hemoglobins, Abnormal
• Aspartic Acid
• Histidine

Topics

• Aspartic Acid
• Female
• Hemoglobins, Abnormal (analysis)
• Histidine
• Humans
• Polycythemia (genetics)