Control of Hemoglobin Function within the Red Cell

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Abstract
HUMAN hemoglobin has probably been studied more carefully than any other protein. The traditional biochemical approach is first to purify a protein and then to study its properties under controlled conditions. Although such methods have proved valuable in correlating the structure and function of hemoglobin, the physiologic interpretation of the data obtained may be tenuous. For example, investigators have wondered for 30 years why the oxygen affinity of whole blood was considerably less than that of hemoglobin in a cell-free solution identical in temperature, pH and ionic strength to that of the red cell. It seemed likely that the red . . .