Oosthuizen M M, Myburgh J A, Schabort J C
Int J Biochem. 1984;16(12):1207-15. doi: 10.1016/0020-711x(84)90218-0.
Acid DNase from monkey liver lysosomes was purified to homogeneity by salt extraction of lysosomal membranes at pH 3.8; (NH4)2SO4 fractionation; low salt precipitation; SP-C50 and G-150 Sephadex chromatography; and polyacrylamide gel electrophoresis. The pH for optimum activity was dual in character with a labile optimum at pH 3.8 and a less active but stable one at pH 4.2. The estimated molecular weight was 40K and the pI was 4.4. Inorganic ions such as Ca2+, Mg2+, Mn2+ and SO2-4 were more than 80% inhibitory at 10-mM levels. Fe3+ ions were 80% inhibitory at 0.1-mM levels. NaCl at 100 mM is essential for activity but becomes 100% inhibitory above 200 mM.
通过在pH 3.8下对溶酶体膜进行盐提取；硫酸铵分级分离；低盐沉淀；SP-C50和G-150葡聚糖凝胶色谱法；以及聚丙烯酰胺凝胶电泳，从猴肝溶酶体中纯化出了酸性脱氧核糖核酸酶，使其达到同质。最佳活性的pH具有双重特性，在pH 3.8时有一个不稳定的最佳值，在pH 4.2时有一个活性较低但稳定的值。估计分子量为40K，pI为4.4。Ca2+、Mg2+、Mn2+和SO2-4等无机离子在10 mM浓度时抑制率超过80%。Fe3+离子在0.1 mM浓度时抑制率为80%。100 mM的NaCl对活性至关重要，但在200 mM以上时抑制率达到100%。
