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JBC, Vol. 250, Issue 20, 8214-8219, Oct, 1975

Purification of Escherichia coli endonuclease specific for apurinic sites in DNA

W. G. Verly and E. Rassart

The endonuclease specific for apurinic sites in DNA has been isolated from Escherichia coli B41 as a pure monomeric protein of 32,000 daltons. The enzyme hydrolyzes a phosphodiester bond near the apurinic sites in double-stranded DNA; it does not hydrolyze untreated DNA and its action on alkylated DNA is restricted to the apurinic sites always present. This enzyme is not endonuclease II which is most probably a mixture of two enzymes, one a glycosidase (Kirtikar, D. M., and Goldthwait, D. A. (1974) Proc. Natl. Acad. Sci. U. S. A. 71, 2022-2026), the other an endonuclease for apurinic sites which is the enzyme isolated in this work.
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