Enthalpy changes of dissociation of hemoglobin solution

Kazuhiko Fujioka, Kuniyasu Nakajima, Yoshihiro Baba, Akihiro Kagemoto, Ryoichi Fujishiro
1981 Netsu Sokutei  
Heats of dilution of aqueous hemoglobin solutions were measured using a flow microcalorimeter at 298.15+0.001K. Thermodynamic quantities for the association-dissociation equilibrium of hemoglobin molecules were derived. In order to obtain values of the heats of dissociation ΔH and the dissociation constant K the treatment of data according to Eq.(5) was carried out using two different methods. In the first method ΔH value is estimated using the dissociation constant K as a reciprocal of the
more » ... ciation constant previously determined by osmometry. In the second one the K and ΔH values are treated as adaptable parameters. The two sets of K and ΔH values so estimated are of comparable order. Furthermore, thermodynamic quantities for the association process of hemoglobin molecules were estimated and proved to be reasonable, compared with those reported by other investigators. NETSUSOKUTEI 8(3) 1981 -91-
doi:10.11311/jscta1974.8.91 fatcat:rz4a73kh2vgu7bcsjbsfqn73di