A deoxyribonuclease that is secreted from an insectivorous plant Drosera adelae was partially purified by column chromatography. The enzyme acted as an endonuclease on double-stranded DNA and generated oligonucleotides with 3' hydroxyl and 5' phosphate ends. The activity of the enzyme was high in the range from pH 3.5 to 5.0. The enzyme seemed to require divalent cations for maximum activity.
|Number of pages||2|
|Journal||Nucleic acids symposium series|
|Publication status||Published - 1997|
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