Open AccessPurification of SI nuclease from takadiastase by affinity chromatography on single-stranded DNA-acrylamide columns
Author(s) -
Hanoch Slor
Publication year - 1975
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/2.4.587
Subject(s) - nuclease , biology , dna , nucleic acid , acrylamide , affinity chromatography , biochemistry , enzyme , monomer , chemistry , polymer , organic chemistry
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.