Differential scanning calorimetry (DSC) and isothermal calorimetric batch technique were used to monitor the heat-induced structural changes and adsorption properties of human immunoglobulin G (IgG), in native and hydrophobized states. The transition temperature (Tmax) and enthalpy of heat-induced conformational changes (ΔcalH) of IgG in solution as well as the enthalpy change accompanying the adsorption of IgG onto hydrophilic silica (ΔadsH), were shown to depend on the degree of the protein hydrophobicity (number of covalently attached alkyl chains). The adsorption enthalpy for all forms of IgG at all surface concentrations was found to be endothermic, that is the process is entropy driven. Factors affecting the IgG adsorption onto silica are discussed.
|Original language||American English|
|Number of pages||10|
|Journal||Journal of Thermal Analysis and Calorimetry|
|State||Published - 2003|
Bibliographical noteFunding Information:
This collaborative study was partially supported by ARIEL and carried out in the frame of Arc-en-Ciel (Keshet) program between Israel and France.
- Enthalpy of adsorption
- Human IgG
- Structural changes