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采用表面等离子体子共振(SPR)传感装置,固定入射角,以波长为变量,以CCD为检测系统,用对金有较强吸附作用的谷胱甘肽(GSH)为基底膜,研究了GSH分别与谷胱甘肽硫转移酶(GST)与小分子GPX模拟酶2-位-碲桥联-β-环糊精(2-TeCD)的动力学过程,计算得GSH与GST的结合常数为2.82×106L/mol;GSH与2-TeCD的结合常数为3.92×102L/mol。结果表明:本方法可以用来评价小分子GPX模拟酶与底物的结合程度,简便快捷,不需标记样品,可以实时监测反应过程,作用后酶与底物易于分离,分离后的酶可以继续使用等优点。
Using surface plasmon resonance (SPR) sensing device, fixed angle of incidence, wavelength as a variable, CCD as the detection system, with a strong adsorption of gold on glutathione (GSH) as the basement membrane, studied GSH was determined by the kinetic process of glutathione S-transferase (GST) and small molecule GPX mimic enzyme 2-position-tellurium bridged-β-cyclodextrin (2-TeCD) Was 2.82 × 106 L / mol. The binding constant of GSH to 2-TeCD was 3.92 × 102 L / mol. The results showed that this method can be used to evaluate the binding degree of small molecule GPX mimic enzyme to substrate. It is simple and rapid. Without labeling samples, the method can be used to monitor the reaction process in real time. After the enzyme and substrate are separated, the enzyme can continue Use and so on.