Liu A M, Li S B, Yu W L, Zhang F, Chen J X, Su P
Lanzhou Institute of Chemical Physics, Chinese Academy of Sciences.
Biochem Int. 1990 Dec;22(6):959-65.
The isolation and purification of methane monooxygenase from a type I methanotroph Methylomonas GYJ3 to near homogeneity is reported. The isoelectric focusing in flat-bed granulated gels has resolved the methane monooxygenase into three protein components. The specific activity of the enzyme is 198.4 n mol per min per mg protein, degree of purification 4.13-fold. Recovery of the focused proteins is high and elution simple. Several purification steps may be omitted from the previously published scheme by other techniques.
报道了从I型甲烷氧化菌甲基单胞菌GYJ3中分离纯化甲烷单加氧酶至接近均一的程度。在平板颗粒凝胶中进行等电聚焦可将甲烷单加氧酶分离为三种蛋白质组分。该酶的比活性为每毫克蛋白质每分钟198.4纳摩尔，纯化倍数为4.13倍。聚焦蛋白质的回收率高且洗脱简单。与其他技术相比，先前发表的方案中的几个纯化步骤可以省略。
