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

Hanoch Slor | Zendy

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Purification 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.

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