Ivanov V A, Tret'iak T M, Gaziev A I, Santalov B F
Biokhimiia. 1980 May;45(5):912-22.
A DNAse was isolated from rat brain and purified 1100-fold using affinity chromatography on a column with DNA-agarose and chromatography on granulated hydroxyapatite. The electrophoretically pure Mg2+, Mn2+-dependent enzyme preparation hydrolyzes the denaturated DNA with a maximal activity at pH 8,4. The optimal terminal concentration of Mg2+ corresponds to the Mg/phosphorus molar ratio of the substrate is 1:2. For Mn2+ this correlation is 1:1. Using the immobilized substrate method, the exonuclease type of DNAse activity has been established. The enzyme activity depends on the state of its SH-groups; the reaction is inhibited by pCMB. The molecular weight of DNAase as determined by gel-filtration through Sephadex G-200 is equal to 60 000.
从大鼠脑中分离出一种脱氧核糖核酸酶（DNAse），并通过在DNA-琼脂糖柱上进行亲和层析以及在颗粒状羟基磷灰石上进行层析，将其纯化了1100倍。这种经电泳纯的Mg2+、Mn2+依赖性酶制剂在pH 8.4时水解变性DNA的活性最大。Mg2+的最佳终浓度对应于底物的Mg/磷摩尔比为1:2。对于Mn2+，该比例为1:1。采用固定化底物法，确定了该DNAse的核酸外切酶活性类型。酶活性取决于其巯基的状态；该反应受对氯汞苯甲酸（pCMB）抑制。通过Sephadex G-200凝胶过滤测定，DNAse的分子量为60000。
