Purification of Escherichia coli endonuclease specific for apurinic sites in DNA.
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.
D000596:Amino Acids / Q000032:analysis; D001080:Apurinic Acid / Q000032:analysis*; D001483:Base Sequence; D004247:DNA / Q000032:analysis*; D003851:Deoxyribonucleases / Q000302:isolation & purification* / Q000378:metabolism; D004720:Endonucleases / Q000302:isolation & purification* / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology; D007700:Kinetics; D008970:Molecular Weight; D011119:Polynucleotides / Q000032:analysis*
D000596:Amino Acids; D011119:Polynucleotides; D001080:Apurinic Acid; D004247:DNA; D003851:Deoxyribonucleases; D004720:Endonucleases