Eremin A N, Savenkova M I, Metelitsa D I
Bioorg Khim. 1986 May;12(5):606-12.
The alterations in the catalytic activity of the horseradish peroxidase after its interaction with antibodies against this enzyme have been studied in buffered solution and in reversed Aerosol OT (AOT) micelles in heptane. The antibodies were obtained by immunizing the rabbits with electrophoretically homogeneous enzyme and were purified by affinity chromatography. In the AOT micelles and mixed micelles containing AOT and Triton X-45, the enzyme interacted with antibodies very rapidly (in less than 5 min), i.e. the micelles did not hinder effective interaction between the enzyme and antibodies. The decrease in the peroxidase catalytic activity upon its interaction with antibodies in a micellar medium was determined by [H2O]/[AOT] ratio, pH and molarity of polar nucleus, as well as by the initial concentration of antibody. In buffered solutions, the decrease n the peroxidase activity of the enzyme--antibody complex was only weakly dependent on pH and molarity of a buffer solution.
已在缓冲溶液和庚烷中的反相气溶胶OT（AOT）胶束中研究了辣根过氧化物酶与抗该酶抗体相互作用后其催化活性的变化。通过用经电泳均一的酶免疫兔子获得抗体，并通过亲和色谱法纯化。在AOT胶束以及含有AOT和 Triton X-45的混合胶束中，酶与抗体的相互作用非常迅速（不到5分钟），即胶束不会阻碍酶与抗体之间的有效相互作用。在胶束介质中，过氧化物酶与抗体相互作用时其催化活性的降低取决于[H2O]/[AOT]比值、极性核的pH值和摩尔浓度，以及抗体的初始浓度。在缓冲溶液中，酶-抗体复合物的过氧化物酶活性降低仅微弱地依赖于缓冲溶液的pH值和摩尔浓度。
