Relation between Escherichia coli endonucleases specific for apurinic sites in DNA and exonuclease III.
Contradictory data have recently been published from two different laboratories on the presence vs absence of an intrinsic endonucliolytic activity of E. coli exonuclease III at apurinic sites in double-stranded DNA. It is shown here that an endonuclease activity of this specificity co-chromatographs exactly with exonuclease III on phosphocellulose and Sephadex G-75 columns, indicating that the endonuclease and exonuclease activities are due to the same enzyme. In addition, another E. coli endonuclease specific for apurinic sites exists, which can be separated from exonuclease III by the same chromatographic procedures.
D001080:Apurinic Acid; D004247:DNA; D003851:Deoxyribonucleases / Q000302:isolation & purification / Q000378:metabolism*; D004720:Endonucleases / Q000302:isolation & purification / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D005092:Exonucleases / Q000302:isolation & purification / Q000378:metabolism*; D011119:Polynucleotides; D013379:Substrate Specificity
D011119:Polynucleotides; D001080:Apurinic Acid; D004247:DNA; D003851:Deoxyribonucleases; D004720:Endonucleases; D005092:Exonucleases