[Heat denaturation of immunoglobin G in monomolecular layers].

Studies were carried out of viscous-elastic properties of monomolecular layers of human immunoglobulin IgG formed at the interface water solutions of NaCl--air within 20 degrees C to 50 degrees C at NaCl concentration in sublayer from 0.3 to 1.0 M. It has been shown that at concentrations from 0.3 to 0.5 M of NaCl IgG macromolecules keep the tertiary structure, and in the region 35 +/- 5 degrees C a conformation transition is observed. The recorded conformation transition is reversible and of entropy nature. At NaCl concentration 0.75 in the sublayer and temperature close to 35 degrees C IgG macromolecules undergo irreversible structural changes due to the destruction of hydrogen and disulfide bonds in IgG molecules. Macromolecules dissociate to fragments with molecular mass 49,000 +/- 2000. At NaCl concentration 1.0 M and temperatures 30-50 degrees C IgG macromolecules of the monolayer are in a dissociated state. Changes in entropy, enthalpy and heat capacity as well as areas occupied by the macromolecules at dense packing, molecular mass and efficient electric dipole moment of the monolayer are calculated.