Identification of tryptophan and tyrosine residues in peptides separated by capillary electrophoresis by their second-derivative spectra using diode-array detection.
The use of diode-array detection allows the non-destructive identification of tryptophan and tyrosine residues in complex peptide mixtures separated by capillary electrophoresis. Second-order derivative spectra of both amino acids show significant differences while zero-order spectra are overlapping to a great extent. A mixture of peptides containing tryptophan and/or tyrosine residues was used to evaluate this method. Tryptic peptide maps of carbonic anhydrase and of the bacterial chaperonin protein GroEL, and of an autodigest of trypsin were characterized for tryptophan- and tyrosine-containing peptides. Automated spectra library search was performed successfully.
Hewlett-Packard, Waldbronn, Germany.
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R
Grimm
A
A
Graf
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DN
Heiger
D000595:Amino Acid Sequence; D004586:Electrophoresis / Q000379:methods*; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D013056:Spectrophotometry, Ultraviolet / Q000379:methods*; D014364:Tryptophan / Q000032:analysis*; D014443:Tyrosine / Q000032:analysis*
D010455:Peptides; D014443:Tyrosine; D014364:Tryptophan