Abstract
A new endodeoxyribonuclease specific to apurinic sites in DNA was purified from vegetative cells of Bacillus subtilis. The enzyme hydrolyzes a phosphodiester bond near the heat-induced apurinic sites in double or single strand DNA; it does not hydrolyze native nor alkylated DNA. The endonuclease has a molecular weight of around 105,000 and consists of four identical subunits. The enzyme requires absolutely Mg2+ for its activity and is inhibited by EDTA. It is completely inhibited by 1 m NaCl or 1 mm p-chloromercurybenzoate. These properties are very different from those of the endonuclease specific to apurinic sites in DNA isolated from B, subtilis by Inoue and Kada and those of endonuclease IV and VI of Escherichia coli.
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