枯草芽孢杆菌DNA脱嘌呤位点特异性内切核酸酶的纯化及性质
Purification and properties of a Bacillus subtilis endonuclease specific for apurinic sites in DNA.
作者信息
Inoue T, Kada T
出版信息
J Biol Chem. 1978 Dec 10;253(23):8559-63.
An endonuclease which hydrolyzes depurinated DNA has been purified from extracts of Bacillus subtilis cells. The endonuclease is a monomeric protein and has a molecular weight of around 56,000. The enzyme is specific for apurinic sites in double-stranded DNA, has a pH optimum at 8.0, and is slightly stimulated with 50 mM NaCl but completely inhibited with 500 mM NaCl. It requires no divalent cations and is insensitive to EDTA; it has no associated exonuclease. These properties are very similar to those of Escherichia coli endonuclease IV, which is also insensitive to EDTA and has no exonuclease activity, and very different from those of the main endonuclease for apurinic sites (endonuclease IV) of the same bacterium.
一种可水解脱嘌呤DNA的核酸内切酶已从枯草芽孢杆菌细胞提取物中纯化出来。该核酸内切酶是一种单体蛋白，分子量约为56,000。该酶对双链DNA中的脱嘌呤位点具有特异性，最适pH值为8.0，50 mM NaCl可轻微刺激其活性，但500 mM NaCl可完全抑制其活性。它不需要二价阳离子，对EDTA不敏感；它没有相关的外切核酸酶活性。这些特性与大肠杆菌核酸内切酶IV非常相似，后者对EDTA也不敏感且无外切核酸酶活性，而与同一细菌中脱嘌呤位点的主要核酸内切酶（核酸内切酶IV）的特性有很大不同。
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