GEORGE C. SCHUSSLER, M.D., F.A.C.P.; HELEN M. RANNEY, M.D.
The discovery of the regulatory effect of organic phosphates on the oxygen affinity of human hemoglobin has clarified several previously mystifying clinical observations. Solutions of human hemoglobin were known for many years to have a higher affinity for oxygen than did normal red blood cells. Benesch, Benesch, and Yu observed that when 2,3-diphosphoglycerate (2,3-DPG), the principal organic phosphate of the red cell, was added to phosphate-free hemoglobin solutions, the oxygen affinity of the hemoglobin decreased to levels encountered in intact erythrocytes (1). They found that 1 mole of deoxyhemoglobin (but not oxyhemoglobin) binds 1 mole of 2,3-DPG; the binding occurs
SCHUSSLER GC, RANNEY HM. Thyroid Hormones and the Oxygen Affinity of Hemoglobin. Ann Intern Med. 1971;74:632–633. doi: 10.7326/0003-4819-74-4-632
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Published: Ann Intern Med. 1971;74(4):632-633.
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