Abstract
OH.-induced covalent peptide-nucleotide adducts have been isolated by reverse-phase chromatography from the enzymic hydrolyzates of gamma-ray irradiated solutions containing double-stranded poly(deoxyadenylic-deoxythymidylic acid) and one of the tripeptides, lysyl-tryptophyl-lysine or lysyl-tyrosyl-lysine. Numerous compounds were formed, resulting presumably from different modes of radical addition. All isomers appeared to have the same general structure peptide-d(ApTpA), based mostly on double-labelling experiments of bases and phosphate groups in DNA. The major adduct fraction obtained from Lys-Trp-Lys and poly(dA-dT) was purified to homogeneity by sequential reverse-phase and ion-exchange chromatography, and characterized spectrally. The pattern of acid and alkaline hydrolysis suggests that thymine is the site of peptide-nucleotide binding in this particular adduct fraction.
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