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通过单链DNA-丙烯酰胺柱亲和层析从胰淀粉酶中纯化S1核酸酶。

Purification of S1 muclease from Takadiastase by affinity chromatography on single-stranded DNA-acrylamide columns.

作者信息

Slor H

出版信息

Nucleic Acids Res. 1975 Apr;2(4):587-93. doi: 10.1093/nar/2.4.587.

Abstract

When S1 nuclease from Takadiastase was partially purified according to previously reported methods, it showed a 10 to 15 fold increase in specificactivity. Although such preparations were highly active on single-stranded DNA, they had traces of activity on native DNA and were contaminated by T1-RNase. The S1 enzyme was further purified by a single step of affinity chromatography on single-stranded DNA-acrylamide column to a final purification of 275-fold. This preparation was free of T1-RNase and had an absolute specificity for single-stranded DNA.

摘要

按照先前报道的方法对栖土曲霉S1核酸酶进行部分纯化时,其比活性提高了10至15倍。尽管这样的制剂对单链DNA具有高活性,但它们对天然DNA有微量活性,并且被T1核糖核酸酶污染。通过在单链DNA-丙烯酰胺柱上进行一步亲和层析,将S1酶进一步纯化至最终纯化倍数为275倍。该制剂不含T1核糖核酸酶,并且对单链DNA具有绝对特异性。

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