Abstract
Ammonium tungstophosphate was used in the thin-layer chromatography of 96 peptides, using ammonium nitrate and nitric acid solutions as eluents. The retention of the dipeptides is mainly governed by an ion-exchange mechanism, whereas adsorption appears to determine the affinity of most tripeptides towards the stationary phase. The affinity sequence of the dipeptides can be predicted from that of the corresponding C-terminal amino acids. The retention of glycine and alanine oligomers increases with increase in the number of amino acid residues. Interesting separations of hydrophilic peptides and, particulary, of the oligomers of glycine and alanine are reported.
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