Rhodes J C, Amlung T W, Miller M S
Department of Pathology and Laboratory Medicine, University of Cincinnati, College of Medicine, Ohio 45267-0529.
Infect Immun. 1990 Aug;58(8):2529-34. doi: 10.1128/iai.58.8.2529-2534.1990.
An elastinolytic proteinase of Aspergillus flavus has been isolated to homogeneity, and its physical and biochemical properties have been characterized. Two purification protocols were compared; an initial step of ion-exchange chromatography was found to be equivalent to ammonium sulfate precipitation at neutral pH. A combination of gel filtration and adsorption chromatographies on the resultant crude enzyme produced highly purified elastase with yields of 5 to 10%. The enzyme is a 23-kilodalton protein with a pI of 7.6. The enzyme activity is markedly inhibited by numerous metal ions. Aspergillus elastase appears to be a metalloproteinase EC 3.4.24.X), as determined by its sensitivity to 1,10-phenanthroline.
黄曲霉的一种弹性蛋白酶已被分离纯化至同质，并对其物理和生化特性进行了表征。比较了两种纯化方案；发现离子交换色谱的初始步骤等同于在中性pH下硫酸铵沉淀。对所得粗酶进行凝胶过滤和吸附色谱相结合的操作，得到了产率为5%至10%的高度纯化的弹性蛋白酶。该酶是一种23千道尔顿的蛋白质，其等电点为7.6。该酶的活性受到多种金属离子的显著抑制。根据其对1,10-菲咯啉的敏感性判断，曲霉弹性蛋白酶似乎是一种金属蛋白酶（EC 3.4.24.X）。
