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

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

H Slor
Free PMC article

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

H Slor. Nucleic Acids Res. 1975 Apr.
Free PMC article

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.

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References

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