Purification and characterization of genetically polymorphic deoxyribonuclease I from human kidney.
Purification and characterization of genetically polymorphic deoxyribonuclease I from human kidney.
复制标题
人肾遗传多态性脱氧核糖核酸酶 I 的纯化和表征。
DOI：
10.1093/oxfordjournals.jbchem.a123578
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发表时间：
1991
影响因子：
2.7
通讯作者：
K. Kishi
中科院分区：
文献类型：
--
作者：
D. Nadano;T. Yasuda;K. Kishi
脱氧核糖核酸酶I （DNase I）用兔抗人尿DNase I抗体和敏感的DNase I活性测定从人肾中纯化约85万倍。在SDS-PAGE上，纯化的肾dna酶I有一个主带，其分子质量估计为38,000 Da。纯化的肾dna酶I的活性依赖于Mg2+和Ca2+的存在。G-Actin和抗尿dna酶I抗体均能抑制其活性。肾dna酶I的性质与尿dna酶I相同。
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.