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- W1566756293 abstract "Abstract A virus-induced enzyme, T2 exonuclease A, has been purified 250-fold from cell-free extracts of Escherichia coli infected with bacteriophage T2e9. In order to obtain large quantities of infected cells for this purpose, a continuous system was devised for growing, infecting, and harvesting cells. The specificity of T2 exonuclease A is characterized by a stepwise attack beginning at the 3'-hydroxyl terminus of a polydeoxyribonucleotide chain and the liberation of 5'-mononucleotides. One molecule of the enzyme appears to remove terminal nucleotide residues randomly rather than to degrade any one polynucleotide chain completely before attacking another. Polynucleotide chains bearing a terminal 3'-phosphoryl group are not degraded by T2 exonuclease A. Dinucleotides terminated with a 5'-phosphomonoester end group are readily cleaved, but removal of the terminal 5'-phosphoryl group reduces the rate of cleavage 9-fold. Removal of the 5'-phosphoryl group from oligonucleotide chains containing 3 nucleotide residues or more does not affect the initial rate of cleavage of phosphodiester bonds. Although oligonucleotides of degree of polymerization less than 100 are degraded at least 100 times more rapidly than heat-denatured DNA, the enzyme has greater affinity for heat-denatured DNA. Because of these circumstances, heat-denatured DNA is a potent competitive inhibitor of the degradation of oligonucleotides. The enzyme has greater affinity for the DNA of bacteriophage T2, which contains glucosylated residues of hydroxymethylcytosine, than it has for a comparable preparation of salmon sperm DNA. However, it appears that the presence of the glucosylated residues decreases the rate of hydrolysis about 20-fold." @default.
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- W1566756293 date "1969-03-01" @default.
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- W1566756293 title "Separation and Characterization of Deoxyribonucleases of Escherichia coli B" @default.
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- W1566756293 doi "https://doi.org/10.1016/s0021-9258(18)91786-2" @default.
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