Removal by transamination and scission of residues from the peptide representing the copper-transport site of serum albumin

Abstract

The peptide Asp-Ala-His-NH-Me was subjected to removal of its N-terminal residue by transamination and scission. Despite the high affinity of the peptide for Cu2+ ions, they catalysed its transamination smoothly. Two main transamination products were found, a complication previously observed with another peptide with an N-terminal aspartic residue, but their scission gave a single product, Ala-His-NH-Me. This was subjected to a further cycle of transamination and scission, and gave a single product after each step. For scission of transaminated peptides it proved unnecessary to remove them from transamination reagents provided that transamination was stopped with EDTA before adding the scission reagent.