SEPARATION OF ACIDIC PROTEIN-TYROSINE KINASE SUBSTRATES BY STRONG ANION-EXCHANGE CHROMATOGRAPHY

A series of heptapeptide sequences containing two glutamic and one asp artic acid residues, synthesized as substrates or inhibitors of differ ent tyrosine kinases, and their phosphorylated or phosphonate analogs, were characterized analytically by strong anion-exchange high-perform ance liquid chromatography. Peptides of slightly different acidity can be separated under the experimental conditions used and the elution o rder 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 prepar ative purification. (C) 1998 Elsevier Science B.V. All rights reserved .