Thermodynamic aspect of the interaction of dichlorotetrafluoroethane with bovine albumin-1.
Binding of dichlorotetrafluoroethane (F 114) with bovine albumin was studied at 37, 20.5 and 5 C. It was found that at the total concentration of 0.4 x 10-3 M of F 114 in the 5-percent protein solution, 50, 51 and 55% of them, respectively, were in bound form at the temperatures indicated above. The termodynamic data found for the F 114-bovine albumin interaction in the temperature range studied were: deltaG = -3.44 to -4.11 Kcal/mol. deltaS =20.40 to 20.45 e.u., and deltaH =2.23 Kcal/mol. It is postulated that the large positive entropic change associated with a sizable positive enthalpy change indicates that the breaking of iceberg water stucture and slight unfolding of albumin molecule are involved in the interaction.
D000335:Aerosol Propellants; D000418:Albumins / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D005465:Fluorocarbon Polymers / Q000378:metabolism*; D005466:Fluorocarbons / Q000378:metabolism*; D011485:Protein Binding; D012995:Solubility; D013696:Temperature
D000335:Aerosol Propellants; D000418:Albumins; D005465:Fluorocarbon Polymers; D005466:Fluorocarbons