Priev A I, Sarvazian A P, Dzantiev B B, Zherdev A V, Cherednikova T V
Mol Biol (Mosk). 1990 May-Jun;24(3):629-37.
The values of apparent adiabatic compressibility of free and antigen-bound antibodies were determined by means of precise density and ultrasound velocity measurements. It was shown that during the formation of soluble immune complexes (insulin--monoclonal antibodies to insulin and alpha-amylase--monovalent Fab-fragments of antibodies to alpha-amylase), the apparent compressibility of antibodies decreased by (0.3 divided by 0.9).10(-6) cm3/g.bar. During the formation of large insoluble aggregates (alpha-amylase--polyclonal antibodies to alpha-amylase), the apparent compressibility decreased by (5.5 +/- 0.7).10(-6) cm3/g.bar. It is suggested that the decrease in the magnitude of thermal fluctuations of the molecular volume of antibodies during antigen binding, manifesting itself by the decrease in their compressibility and strengthened several-fold by precipitate formation, may favour the activation of the effectory functions of antibodies.
通过精确的密度和超声速度测量，测定了游离抗体和抗原结合抗体的表观绝热压缩率值。结果表明，在可溶性免疫复合物（胰岛素 - 抗胰岛素单克隆抗体以及α-淀粉酶 - 抗α-淀粉酶单价Fab片段）形成过程中，抗体的表观压缩率降低了(0.3÷0.9)×10⁻⁶ cm³/g·bar。在大的不溶性聚集体（α-淀粉酶 - 抗α-淀粉酶多克隆抗体）形成过程中，表观压缩率降低了(5.5±0.7)×10⁻⁶ cm³/g·bar。有人提出，抗原结合过程中抗体分子体积热涨落幅度的减小，表现为其压缩率降低，并因沉淀形成而增强数倍，这可能有利于抗体效应功能的激活。
