The reaction of inositol hexaphosphate with hemoglobin |
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| Authors: | Q H Gibson R D Gray |
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| Affiliation: | 1. Upstate Medical University, State University of New York, Syracuse, NY, USA;2. University of Minnesota Medical Center, Minneapolis, MN, USA;3. Brigham and Women''s Hospital, Boston, MA, USA;4. Bayer HealthCare Pharmaceuticals, Whippany, NJ, USA;5. University of California, Davis, Sacramento, CA, USA |
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| Abstract: | The rate of oxygen dissociation from the fully liganded hemoglobin tetramer (Hb4(O2)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 Hb4(O2)4. Inositol hexaphosphate does not, however, modify the rate of CO dissociation from Hb4(CO)4 but it does decrease the rate of CO binding to Hb4(CO)3 by about seven-fold compared to the phosphate-free system. |
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