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J Skerjanc

Publications and source records attributed to J Skerjanc.

4 recordsLinked to original sources

Thermodynamics of the isothermal interaction of human immunoglobulin G with guanidinium chloride.

A thermodynamic study of the isothermal interaction of human immunoglobulin G with guanidinium chloride, a strong denaturant, has been performed. Free energies of interaction were calculated using preferential binding data obtained by measuring densities at constant chemical potential and constant composition, respectively. Enthalpies of interaction were determined calorimetrically. The values of both thermodynamic parameters as well as those of entropies of interaction have been found to depend crucially on the extent of denaturant binding.

Guanidines

Thermodynamics of the isothermal interaction of beta-lactoglobulin with guanidinium chloride and urea.

A thermodynamic study of the isothermal interaction of beta-lactoglobulin with guanidinium chloride and urea has been performed. Enthalpies of interaction of the two denaturants have been obtained by calorimetric measurements, and the free energy of interaction calculated from previously determined preferential binding of denaturants. In separate dilatometric experiments the volume changes accompanying the interaction of guanidinium chloride with beta-lactoglobulin have also been determined.

Binding Sites

Thermodynamic properties of polyelectrolyte solutions containing mixtures of monovalent and trivalent counterions.

The osmotic coefficients, heats of dilution, and volume changes on dilution of aqueous solutions containing mixtures of polystyrenesulfonic acid and its lanthanum salt have been determined at 25 degrees C. The curve representing the osmotic coefficient as a function of the equivalent fraction of the acid has a maximum; the corresponding curves for the enthalpy and volume changes on dilution have a sigmoidal shape. Experimental results have been compared with predictions of the theory based on the cell model with cylindrical symmetry. A semiquantitative agreement between theory and experiment has been found.

Electrolytes

Dilatometry, a neglected method in immunological studies.

Dilatometry has become a useful method for the study of proteins owing to its simplicity and accuracy. However, it has seldom been used in the study of immunoglobulins. Therefore possible applications of the method for that study are being discussed. A description is also given of the most common experimental set-up and procedure for dilatometric experiments. Finally, several papers describing the application of dilatometry to the study of immunoglobulins are reviewed.

Antigen-Antibody Reactions