Nadano D, Yasuda T, Kishi K
Department of Legal Medicine, Fukui Medical School.
J Biochem. 1991 Sep;110(3):321-3. doi: 10.1093/oxfordjournals.jbchem.a123578.
Deoxyribonuclease I (DNase I) was purified about 850,000-fold from human kidney using a rabbit anti-human urine DNase I antibody and sensitive DNase I activity assay. On SDS-PAGE, the purified kidney DNase I gave a single major band, and its molecular mass was estimated to be 38,000 Da. The activity of purified kidney DNase I was dependent on the presence of Mg2+ and Ca2+. G-Actin inhibited the activity, as did the anti-urine DNase I antibody. The properties of the kidney DNase I were the same as those of urine DNase I.
使用兔抗人尿脱氧核糖核酸酶I（DNase I）抗体和灵敏的DNase I活性测定法，从人肾脏中纯化出了约850,000倍的脱氧核糖核酸酶I。在十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（SDS-PAGE）上，纯化的肾脏DNase I呈现出一条单一的主要条带，其分子量估计为38,000道尔顿。纯化的肾脏DNase I的活性依赖于镁离子（Mg2+）和钙离子（Ca2+）的存在。G-肌动蛋白抑制其活性，抗尿DNase I抗体也有同样的作用。肾脏DNase I的特性与尿DNase I的特性相同。
