Summary
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.