Could capillary zone electrophoresis of tryptic peptides be used for the characterization of hemoglobin variants?

The present article describes a simple and rapid new peptide mapping proced ure that could be used to assist identification of rare hemoglobin variants in clinical laboratories. Four hemoglobin variants were taken as example, namely Hb D-Ouled Rabah, Hb Marseille, Hb G-Philadelphia, and Hb Ube-2, and isolated by electrophoresis at alkaline pH. The globin chains were aminoet hylated and, after tryptic digestion, the peptides were separated by a capi llary zone electrophoresis method. Highly reproducible migration times of t he peptides were obtained with intra-assay and inter-assay coefficients of variation of less than 1 and 2%, respectively.