Spin-label detection of hemoglobin-membrane interaction at physiological pH

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Abstract
The interaction between hemoglobin and the cytoplasmic surface of human erythrocyte membranes at physiological pH was studied by monitoring the electron paramagnetic resonance (EPR) signal of spin-labeled membrane ghosts in hemoglobin solutions of various concentrations. The EPR spectra indicate the existence of a significant hemoglobin-membrane interaction which exhibits a substantial hemoglobin concentration dependence over the concentration range 0-12 mg/mL. An equilibrium binding model yields a hemoglobin-membrane dissociation constant, Kd, on the order of 10(-4) M, at and above physiological pH; the interaction is classified as very low-affinity binding. The interaction increases significantly when the pH is decreased. Half-saturation of the binding sites occurs at a ratio of about 10(8) hemoglobins per cell.

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