Purification of S1 muclease from Takadiastase by affinity chromatography on single-stranded DNA-acrylamide columns.
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.
D000178:Acrylamides; D000681:Amylases / Q000032:analysis; D016282:Aspartic Acid Endopeptidases; D001230:Aspergillus / Q000201:enzymology*; D002846:Chromatography, Affinity; D002848:Chromatography, DEAE-Cellulose; D004277:DNA, Single-Stranded; D003851:Deoxyribonucleases / Q000302:isolation & purification*; D006863:Hydrogen-Ion Concentration; D014908:Triticum
D000178:Acrylamides; D004277:DNA, Single-Stranded; D003851:Deoxyribonucleases; D000681:Amylases; D016282:Aspartic Acid Endopeptidases; C022772:Aspergillus oryzae carboxyl proteinase