‘ De novo’ sequencing of Atlantic cod vitellogenin tryptic peptides by matrix‐assisted laser desorption/ionization quadrupole time‐of‐flight tandem mass spectrometry: similarities with haddock vitellogenin

• Published in: Rapid Communications in Mass Spectrometry
• Main Authors: Cohen, Alejandro M., Mansour, Atef A. H., Banoub, Joseph H.
• Format: Article in Journal/Newspaper
• Language: English
• Published: Wiley 2005
• Subjects: atlantic cod; Gadus morhua
• Online Access: http://dx.doi.org/10.1002/rcm.2084; https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Frcm.2084; https://onlinelibrary.wiley.com/doi/full/10.1002/rcm.2084

Abstract Vitellogenin is a protein produced by the liver of oviparous animals in response to circulating estrogens. The amino acid sequence of vitellogenin from Atlantic cod ( Gadus morhua ) has not yet been determined. In this study Atlantic cod vitellogenin was characterized using a ‘bottom‐up’ mass spectrometric approach. Vitellogenin synthesis was induced ‘ in vivo ’ with β ‐estradiol, and subjected to trypsin digestion for characterization by matrix‐assisted laser desorption/ionization quadrupole time‐of‐flight tandem mass spectrometry. A peptide mass fingerprint was obtained and ‘ de novo ’ sequencing of the most abundant tryptic peptides was performed by low‐energy collision‐induced dissociation tandem mass spectrometry. As a result of these experiments, the sequences of various tryptic peptides have been elucidated. The database search has shown that Atlantic cod vitellogenin shares a series of common peptides with the two different known vitellogenin sequences of haddock, a closely related species. These findings allow us to propose that Atlantic cod might also co‐express at least two distinct forms of vitellogenin. Copyright © 2005 John Wiley & Sons, Ltd.