Date Published:
2003///Abstract:
Differential scanning calorimetry (DSC) and isothermal calorimetric batch technique were used to monitor the heat-induced structural changes and adsorption properties of human IgG, in native and hydrophobized states. The transition temp. (Tmax) and enthalpy of heat-induced conformational changes (ΔcalH) of IgG in soln. 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 (no. of covalently attached alkyl chains). The adsorption enthalpy for all forms of IgG at all surface concns. was found to be endothermic, that is the process is entropy driven. Factors affecting the IgG adsorption onto silica are discussed. [on SciFinder(R)]Notes:
CAPLUS AN 2003:91834(Journal)