Abstract
A series of heptapeptide sequences containing two glutamic and one aspartic acid residues, synthesized as substrates or inhibitors of different tyrosine kinases, and their phosphorylated or phosphonate analogs, were characterized analytically by strong anion-exchange high-performance liquid chromatography. Peptides of slightly different acidity can be separated under the experimental conditions used and the elution order increased in parallel with the number of acidic functions present in the sequence. The eluents and the characteristics of strong anion-exchange columns permit the scale-up of the method described to preparative purification.
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