超氧化物歧化酶活性的测定

Determination of superoxide dismutase (SOD) activity

主要采用光谱法研究测定超氧化物歧化酶(SOD)活性及不同实验条件对其活性的影响,找出最优的测活条件,为实际工作提供一些有意义的指导,并且为下一步的酶促反应动力学研究提供实验和理论依据.实验结果表明,测定SOD活性的最优条件为:实验温度为25℃,0.1mol.L-1 Tris-HCl缓冲溶液,pH值为8.20,内含2.0mmol.L-1 EDTA,邻苯三酚浓度为2.5mmol.L-1,控制酶的加入量为0.30mL.

SOD activity and the effects of different experimental conditions on SOD activity were measured by spectral method.The optimum conditions were obtained.This was helpful to supply the experimental data and theoretical basis with the enzyme kinetics.The results indicated that the optimum conditions were as follow,constituents and concentration of the buffer:Tris-HCl,0.1 mol·L-1;pH=8.20;EDTA,2.0 mmol·L-1;conducted at 25 ℃;the concentration of the adjacent pyrogallol:2.5 mmol·L-1;control enzymes adding level at 0.3 mL.