Principal component analysis of mass spectra of peptides generated from the tryptic digestion of protein mixtures

• Published in: Rapid communications in mass spectrometry 2001-01, Vol.15 (6), p.418-427
• Main Authors: Bryant, Duncan K., Monté, Soraya, Man, Wai J., Kramer, Kerstin, Bugelski, Peter, Neville, William, White, Ian R., Camilleri, Patrick
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; Electrophoresis, Polyacrylamide Gel; Glutathione Transferase - metabolism; Histamine H1 Antagonists - toxicity; Liver - chemistry; Male; Methapyrilene - toxicity; Molecular Sequence Data; Peptide Mapping; Peptides - analysis; Peptides - chemistry; Peptides - metabolism; Peroxisomes - metabolism; Rats; Rats, Sprague-Dawley; Spectrometry, Mass, Electrospray Ionization; Trypsin - metabolism
• ISSN: 0951-4198; 1097-0231
• DOI: 10.1002/rcm.247

Principal component analysis (PCA) has been used to analyse mass spectral peptide profiles obtained from the enzymatic digestion of standard protein mixtures. Scores and loadings plots clearly revealed peptide fragments that differentiated one protein mixture from another. Peptide map search results identified with a high degree of certainty any additional proteins in these mixtures. As a proof‐of‐concept this methodology was applied to hepatic protein mixtures obtained from rats treated with two hepatotoxic compounds: methapyriline and SB‐219994. Liver proteins were extracted, pre‐separated by one‐dimensional polyacrylamide gel electrophoresis, subjected to tryptic digestion and analysed by mass spectrometry. Two up‐regulated proteins, glutathione S‐transferase with methapyrilene and peroxisomal bifunctional enzyme with SB‐219994, were identified in this manner. Copyright © 2001 John Wiley & Sons, Ltd.