Breter H J, Schmidt B, Zahn R K
Enzyme. 1975;19(3):149-53. doi: 10.1159/000458986.
A four-step procedure for purification of a nuclease from the keratinous sponge Verongia aerophoba is described. The extracted material is lyophilized, acidified, and subjected to chromatography on Sephadex, hydroxyapatite, and phosphocellulose. The nuclease is purified about 1,000-fold from the crude extract and approximately 1,600-fold from concomitant acid RNase. Phosphodiesterase is lost after chromatography on Sephadex. The purified enzyme solution contains one single activity as determined by polyacrylamide gel electrophoresis.
描述了从角质海绵Verongia aerophoba中纯化核酸酶的四步程序。提取的材料经冻干、酸化后,在葡聚糖凝胶、羟基磷灰石和磷酸纤维素上进行层析。核酸酶从粗提物中纯化了约1000倍,从伴生的酸性核糖核酸酶中纯化了约1600倍。磷酸二酯酶在葡聚糖凝胶层析后丧失。通过聚丙烯酰胺凝胶电泳测定,纯化的酶溶液含有单一活性。