Oxygen equilibrium of hemoglobin J Cape Town.

Abstract

Polycythemia in carriers of hemoglobin J Cape Town or hemoglobin Chesapeake is thought to be produced by increased oxygen affinity of their blood. Both hemoglobins involve substitution of amino acid residue alpha FG-4. Measurements reported here, of the oxygen equilibrium of purified hemoglobin J Cape Town, permit direct comparison of the two hemoglobins. J Cape Town exhibits lower oxygen affinity, and greater heme-heme interaction, than Chesapeake; both exhibit normal Bohr effects. Substitution of one polar amino acid residue for another of opposite charge (arginine --> glutamic acid) thus appears to create less disruption of the interface between alpha- and beta-chains than substitution of a nonpolar residue (arginine --> leucine).

• Authors: S Charache, T Jenkins
• Journal: The Journal of clinical investigation (J Clin Invest) Vol. 50 Issue 7 Pg. 1554-5 (Jul 1971) ISSN: 0021-9738 [Print] United States
• PMID: 5090068 (Publication Type: Journal Article)

Chemical References

• Hemoglobins, Abnormal
• Heme
• Oxygen

Topics

• Amino Acid Sequence
• Blood Protein Electrophoresis
• Heme (metabolism)
• Hemoglobins, Abnormal (metabolism)
• Humans
• Hydrogen-Ion Concentration
• Oxygen (blood)
• Polycythemia (blood)