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Biophysical Journal 9: 36-53 (1969)
© 1969 the Biophysical Society
ABSTRACT
By continuous absorption and by bubble collapse methods respectively, the solubilities and diffusion coefficients of oxygen in water and in dilute solutions of human hemoglobin (1.11, 2.22, and 4.44 wt%) have been determined at one atmosphere and 10°, 20°, 30°, 40°, 50°, and 60°C. Measured equilibrium constants, oxygen/hemoglobin ratios and isochoric heats of solution have been interpreted in terms of various mechanisms for oxygen-hemoglobin interaction. Oxygen diffusivities obtained experimentally for the hemolyzed blood solutions have been found to compare favorably with those predicted by a model of facilitated transport proposed by Houghton (1966). The diffusion measurements indicate that, while kinetic phenomena cannot be ignored, the over-all rate of exchange of oxygen with hemoglobin is not a controlling factor in facilitated diffusion. Anomalous equilibrium constants and temperature coefficients have been observed in the most dilute hemoglobin solution at the lowest temperatures.
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