Purification of SI nuclease from takadiastase by affinity chromatography on single-stranded DNA-acrylamide columns
Open Access
- 1 January 1975
- journal article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 2 (4) , 587-593
- https://doi.org/10.1093/nar/2.4.587
Abstract
When SI nuclease from Takadiastase was partially purified according to previously reported methods, it showed a 10 to 15 fold increase in specific-activity. Although such preparations were highly active on single-stranded DNA, they had traces of activity on native DNA and were contaminated by TI-RNase. The SI 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 Tl-RNase and had an absolute specificity for single-stranded DNA.Keywords
This publication has 2 references indexed in Scilit:
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- A nuclease specific for heat-denatured DNA isolated from a product of Aspergillus oryzaeBiochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1966