Chasovnikova L V, Matveeva N A, Lavrent'ev V V
Biofizika. 1982 May-Jun;27(3):435-40.
Resistance to surface denaturation of human and horse immunoglobulin G (IgG) molecules at aqueous NaCl solution--octane interface as a function of aqueous phase pH and NaCl concentration has been studied by monomolecular layer method. Higher conformational stability of these proteins at oil--water interface as compared to that at air-water interface has been demonstrated. At aqueous solutions of 0.15 M NaCl concentration and pH range from 2.8 to 8.0 units no conformational changes were fixed. With the change of NaCl concentration in aqueous phase from 0.15 to 2.0 M at neutral pH horse IgG molecules did not lose their native conformation. Human IgG molecules were only slightly undergoing denaturation process under the same conditions.
采用单分子层法研究了人及马免疫球蛋白G（IgG）分子在NaCl水溶液 - 辛烷界面的表面变性抗性与水相pH值和NaCl浓度的关系。已证明这些蛋白质在油 - 水界面的构象稳定性高于在气 - 水界面的构象稳定性。在0.15 M NaCl浓度和pH值范围为2.8至8.0单位的水溶液中，未观察到构象变化。在中性pH值下，当水相中NaCl浓度从0.15 M变为2.0 M时，马IgG分子未丧失其天然构象。在相同条件下，人IgG分子仅轻微经历变性过程。
