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The oxygenation of hemoglobin is under the control of the regulatory function of organic phosphates. The one in mammals corresponds to 2,3‐bisphosphoglycerate but in birds and turtles appears to be inositol hexakisphosphate. The latter component decreases the oxygen affinity of the two chicken hemoglobin compounds (the minor and the major) and the lone pigeon hemoglobin component. The Bohr effects have also been determined for the two hemoglobin samples. As has already been observed by electrophoresis and by chromatography, pigeon hemoglobin seems to behave more like that of the major chicken component by disclosing analogous log p50 values, i.e. the partial pressure of oxygen corresponding to a 50% load of the hemoglobin.

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