PMID: 1203242Dec 30, 1975Paper

The investigation of peptide-oligodeoxythymidylic acid interactions using template chromatography

Biochemistry
H SchottE Bayer

Abstract

Poly(vinyl alcohol) has been substituted with oligodeoxythymidylic acid and the resulting polyanion irreversibly attached to DEAE-cellulose via ionic bonding. Peptide-oligonucleotide interactions have been studied using a column chromatography technique with the PV(pT)n-DEAE-cellulose as stationary phase. Of all the naturally occurring amino acids, only tryptophan and to a lesser extent tyrosine intreact significantly with the immobilized oligodeoxythymidylic acid residues under the conditions for base pairing. The homopolymers of tryptophan and tyrosine undergo greater retardation than the monomers, such that the effect is not additive but multiplicative. Thus Tyr-Tyr-Tyr shows an eightfold and Trp-Trp-Trp an approximately 30-fold larger retardation than tyrosine and tryptophan, respectively. The peptide-oligonucleotide interaction decreases considerably when nonaromatic amino acids are present in the peptide. Consequently, naturally occurring peptides and proteins which contain relatively small amounts of tryptophan and tyrosine compared with the nonaromatic amino acids undergo at the most only slight retardation on the PV(pT)n-DEAE-cellulose. The retention of oligonucleotides and peptides containing these aromatic amino acid...Continue Reading

References

May 24, 1974·Biochimica Et Biophysica Acta·F Morita
Jun 1, 1972·Angewandte Chemie·K L AgarwalH G Khorana
Jul 1, 1974·European Journal of Biochemistry·K G Wagner, H A Arfmann

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Citations

Mar 1, 1979·Archives of Biochemistry and Biophysics·N A NicolaG D Fasman
Jan 1, 1981·CRC Critical Reviews in Biochemistry·C Helene, J C Maurizot
May 1, 1981·International Journal of Peptide and Protein Research·H Eckstein, E Bayer

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