Purification of SI nuclease from takadiastase by affinity chromatography on single-stranded DNA-acrylamide columns

Hanoch Slor*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish
Pages (from-to)587-593
Number of pages7
JournalNucleic Acids Research
Volume2
Issue number4
DOIs
StatePublished - Apr 1975

Funding

FundersFunder number
Israel Cancer Assoc.

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