Abstract
An automated tandem high-performance liquid chromatographic system was developed for peptide mapping of very large proteins. The method was applied systematically to the peptide mapping analysis of four genetic variants of human serum albumin, and amino acid substitutions in three of them could be identified. In two variants the amino acid substitutions were identified in both homozygote and heterozygote specimens. By this peptide mapping method at least 80% of the total amino acid residues can be screened rapidly. The method is especially useful for establishing the molecular basis of genetic relationships among protein variants found in different populations.
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