Abstract
The rate of oxygen dissociation from the fully liganded hemoglobin tetramer (Hb 4(O 2) 4) is increased by the presence of inositol hexaphosphate from approximately 50/sec to 180/sec at 22°. It follows from this observation that inositol hexaphosphate is bound by oxygen-saturated human hemoglobin. This result is in marked contrast to absence of an effect of 2,3-diphosphoglycerate or pyridoxal phosphate on the rate of oxygen dissociation from Hb 4(O 2) 4. Inositol hexaphosphate does not, however, modify the rate of CO dissociation from Hb 4(CO) 4 but it does decrease the rate of CO binding to Hb 4(CO) 3 by about seven-fold compared to the phosphate-free system.
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