Sitaĭlo S Z, Babichev V V, Skripal' I G
Mikrobiol Zh (1978). 1993 Jan-Feb;55(1):12-8.
Nonspecific endogenic DNAase has been isolated from biomass of Mycoplasma fermentans PG-18 cells and purified to the homogeneous state. The scheme of isolation consists of purification stages on columns with phosphocellulose, DNA-cepharose CL-8B and phenylcepharose. DNAase was not bound to phosphocellulose, its volume was equal to zero. Then this DNAase was passed through column with DEA-cepharose CL-6B (elution by gradient KCl from 0.1 to 1.8M): enzyme was eluted at KCl concentration in the eluting buffer from 0.1 to 1.2 M. The enzyme was purified to the homogeneous state on column with phenylcepharose (elution by linear gradient of ethylene glycol from 30 to 80%): enzyme was eluted at the concentration of ethylene glycol in the eluting buffer from 43 to 80%. According to data obtained using gel-electrophoresis, under the denaturing conditions molecular mass of enzyme in acrylamide gel was 34 kDa.
非特异性内源性脱氧核糖核酸酶已从发酵支原体PG - 18细胞的生物质中分离出来并纯化至均质状态。分离方案包括在磷酸纤维素柱、DNA - 琼脂糖凝胶CL - 8B柱和苯基琼脂糖柱上的纯化阶段。脱氧核糖核酸酶不与磷酸纤维素结合，其体积为零。然后将该脱氧核糖核酸酶通过DEA - 琼脂糖凝胶CL - 6B柱（用0.1至1.8M的KCl梯度洗脱）：酶在洗脱缓冲液中KCl浓度为0.1至1.2M时被洗脱。该酶在苯基琼脂糖柱上纯化至均质状态（用30%至80%的乙二醇线性梯度洗脱）：酶在洗脱缓冲液中乙二醇浓度为43%至80%时被洗脱。根据使用凝胶电泳获得的数据，在变性条件下，丙烯酰胺凝胶中酶的分子量为34 kDa。
