Sanchez-Moreno M, Entrala E, Janssen D, Osuna A
Department of Biochemistry and Molecular Biology Faculty of Sciences, University of Granada, Spain.
Biosci Rep. 1994 Apr;14(2):83-90. doi: 10.1007/BF01210303.
Copper-zinc superoxide dismutase from Ascaris suum (Nematoda) was purified in a new, more efficient, and faster manner. The process included differential centrifugation, fractionation with ammonium sulfate, and sodium dodecyl sulfate-polyacrylamide electrophoresis, yielding a 340-fold purification (specific activity of 47 units/mg). Optimal storage conditions, optimal pH range, thermostability, molecular weight and ultraviolet-visible absorption spectrum of the enzyme are described, and a new enzymatic model for pharmacological screening is suggested.
来自猪蛔虫(线虫纲)的铜锌超氧化物歧化酶以一种全新、更高效且更快的方式得到了纯化。该过程包括差速离心、硫酸铵分级分离以及十二烷基硫酸钠 - 聚丙烯酰胺凝胶电泳,得到了340倍的纯化效果(比活性为47单位/毫克)。文中描述了该酶的最佳储存条件、最佳pH范围、热稳定性、分子量以及紫外 - 可见吸收光谱,并提出了一种用于药理筛选的新酶学模型。