1887

Abstract

An endodeoxyribonuclease specific to apurinic sites in DNA was purified 12000-fold from vegetative cells of the anaerobic thermophilic bacterium, strain IFO 13698. The enzyme specifically hydrolyses phosphodiester bonds of apurinic double-stranded DNA, without action on normal, alkylated, or single-stranded depurinated DNA. The endodeoxyribonuclease has a molecular weight of about 18500 and a sedimentation value of 2.2S. The enzyme has an optimum pH of 7.5.80 and an optimum temperature of 55 °C. The half-life of purified enzyme is 55 min at 60 °C but it can be heated at 60 °C for at least 60 min without loss of activity in the presence of BSA. The purified enzyme has an absolute requirement for Mg or Mn, and is inhibited by EDTA. Enzyme activity is completely inhibited by 0-5 M-NaCl or 1 mM--chloromercuribenzoate. All these properties differ from those of apurinic/apyrimidinic endodeoxyribonucleases isolated from . and .

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/content/journal/micro/10.1099/00221287-130-6-1525
1984-06-01
2019-10-19
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http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-130-6-1525
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