Purification of S1 muclease from Takadiastase by affinity chromatography on single-stranded DNA-acrylamide columns.
Nucleic Acids Res, 1975/4;2(4):587-93.
PMID: 237256
Impact factor: 19.16
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.
MeSH terms
Acrylamides; Amylases; Aspartic Acid Endopeptidases; Aspergillus; Chromatography, Affinity; Chromatography, DEAE-Cellulose; DNA, Single-Stranded; Deoxyribonucleases; Hydrogen-Ion Concentration; Triticum
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