Chasovnikova L V, Matveeva N A, Lavrent'ev V V
Biofizika. 1982 Jan-Feb;27(1):17-9.
Orientation, resistance to surface denaturation and surface potential of bovine and horse immunoglobulin G (IgG) and also of pig IgG-antibodies against DNP and DNS groups on the surface of NaCl solutions of various concentrations have been studied by monomolecular layer method. High conformational stability of IgG molecules of all the species was confirmed. At the surface of NaCl solutions with concentrations 0.15--0.5 M immunoglobulins of all species from monolayers consisting of practically non-unfolded molecules with such an orientation, that all the fragments of IgG molecule are located horizontally. Beyond the limits of this native structure stability zone the rate of surface denaturation is directly proportional to NaCl concentration in the solution. The values of surface potentials of all immunoglobulins under study are close to each other and change little with the surface denaturation.
采用单分子层法研究了牛、马免疫球蛋白G（IgG）以及猪抗DNP和DNS基团IgG抗体在不同浓度NaCl溶液表面的取向、抗表面变性能力和表面电位。证实了所有物种的IgG分子具有高构象稳定性。在浓度为0.15 - 0.5M的NaCl溶液表面，所有物种的免疫球蛋白形成由几乎未展开的分子组成的单分子层，其取向使得IgG分子的所有片段均水平排列。超出该天然结构稳定区范围，表面变性速率与溶液中NaCl浓度成正比。所研究的所有免疫球蛋白的表面电位值彼此接近，并且随着表面变性变化不大。
