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- W2013918905 abstract "Restriction endonuclease R·Eco K catalyzes the cleavage of unmodified bacteriophage λ-DNA leaving 3′-hydroxyl and 5′-phosphoryl groups. This is inferred from the observation that polynucleotide kinase transfers 32P from [γ-32P]-ATP to the 5′-termini of cleaved DNA only after dephosphorylation with bacterial alkaline phosphatase. The extent of such transfer indicates that restriction endonuclease R·Eco K makes approximately three or four double-strand cuts in unmodified λ-DNA under the conditions employed. However, analysis of the terminal 5′-mononucleotides shows that cleavage does not occur at unique sequences." @default.
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- W2013918905 date "1979-12-01" @default.
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- W2013918905 title "Nonspecific cleavage by restriction endonuclease R·Eco K of bacteriophage λ-DNA" @default.
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- W2013918905 doi "https://doi.org/10.1016/0006-2944(79)90013-9" @default.
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