Suppr超能文献

[大肠杆菌多核苷酸磷酸化酶的分离及某些性质]

[Isolation and some properties of polynucleotide phosphorylase from E. coli].

作者信息

Bagdonas A S, Sabaliauskene V L, Iuodka B A

出版信息

Biokhimiia. 1981 May;46(5):802-8.

PMID:7028138
Abstract

A new method for isolation of polynucleotide phosphorylase from E. coli, including ion-exchange chromatography and gel-filtration has been developed. The method results in 300-fold purification of the enzyme, which being devoid of nuclease and phosphatase activities can further be utilized for oligonucleotide synthesis. It was shown that upon storage the enzyme loses the primer-independent activity and in the absence of NaCl can be used for further syntheses. An addition of NaCl stimulates the elongation of the oligonucleotide chain. Some advantages of polynucleotide phosphorylase from E. coli in comparison with the M. luteus enzyme are discussed.

摘要

已开发出一种从大肠杆菌中分离多核苷酸磷酸化酶的新方法,包括离子交换色谱法和凝胶过滤法。该方法可使该酶纯化300倍,该酶无核酸酶和磷酸酶活性,可进一步用于寡核苷酸合成。结果表明,该酶在储存时会失去不依赖引物的活性,在没有氯化钠的情况下可用于进一步合成。添加氯化钠可刺激寡核苷酸链的延伸。文中讨论了大肠杆菌多核苷酸磷酸化酶相对于藤黄微球菌酶的一些优点。

相似文献

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验