Nagi M N, al-Bekairi A M, al-Sawaf H A
Department of Pharmacology, College of Pharmacy, King Saud University, Riyadh, Saudi Arabia.
Biochem Mol Biol Int. 1995 Jul;36(3):633-8.
A new spectrophotometric assay of superoxide dismutase (SOD) is described. The assay is based on the SOD-mediated inhibition in the rate of nitroblue tetrazolium reduction to the blue formazan at alkaline pH. The optimized assay of SOD is performed in 50 mM glycine-NaOH buffer, pH 9.5, at 25 degrees C. The SOD concentration is determined from the V/v ratio of rates measured in the absence (V) or the presence (v) of SOD. One unit of SOD has been defined as the concentration that decrease the rate to 50% (V/v = 2). The assay is simple, sensitive, uses commercially available reagents, rapid and easy to perform and could be used routinely for monitoring superoxide dismutase levels in purified protein fractions.
本文描述了一种新的超氧化物歧化酶（SOD）分光光度测定法。该测定法基于在碱性pH条件下，SOD介导抑制硝基蓝四氮唑还原为蓝色甲臜的速率。优化后的SOD测定在25℃、pH 9.5的50 mM甘氨酸 - NaOH缓冲液中进行。SOD浓度由在无SOD（V）或有SOD（v）存在时测得的速率的V/v比值确定。1个SOD单位定义为使速率降低至一半（V/v = 2）的浓度。该测定法简单、灵敏，使用市售试剂，快速且易于操作，可常规用于监测纯化蛋白组分中超氧化物歧化酶的水平。
