A model of the pH-dependence of the number of oxygen-linked chloride binding sites in hemoglobin.
A model is presented of the pH-dependence of the number of oxygen-linked chloride binding sites established by nuclear magnetic resonance quadrupole-relaxation studies on various mutant and chemically modified hemoglobins. The predictions of the model are in good qualitative agreement with the measured pH-dependences of the linewidth of the 35Cl- NMR signal. The obtained agreement implies that more chloride is bound to oxygenated than to deoxygenated hemoglobin.
D002712:Chlorides; D006454:Hemoglobins; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D008433:Mathematics; D010108:Oxyhemoglobins; D011485:Protein Binding
D002712:Chlorides; D006454:Hemoglobins; D010108:Oxyhemoglobins