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Oxygen binding to sickle cell hemoglobin.
Authors:S J Gill  R C Benedict  L Fall  R Spokane  J Wyman
Affiliation:Department of Chemistry University of Colorado Boulder, Col. 80309, U.S.A.;Institutes of Chemistry and Biochemistry Faculty of Medicine University of Rome Rome, Italy
Abstract:The extent of oxygen binding and light scattering of concentrated solutions of hemoglobin S have been determined as a function of oxygen partial pressure using a thin film optical cell. Nearly reversible oxygen binding is observed as witnessed by the small hysteresis found between slow deoxygenation and reoxygenation runs. High co-operativity is noted from unusually large concentration-dependent Hill coefficients when aggregated hemoglobin S is present. The application of linkage theory with the inclusion of non-ideal solution properties permits a test of various simple models for oxygen binding to both the monomer (α2β2s) and polymer (aggregated) phase. It is concluded that oxygen binding to the polymer is either negligible or small under present experimental conditions. Phase diagrams of the solution concentration in equilibrium with polymer phase as a function of oxygen partial pressure are derived using best fit values of polymer parameters.
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