Characterisation of the intact rainbow trout vitellogenin protein and analysis of its derived tryptic and cyanogen bromide peptides by matrix-assisted laser desorption/ionisation time-of-flight-mass spectrometry and electrospray ionisation quadrupole/time-of-flight mass spectrometry

Joseph Banoub, Pierre Thibault, Atef Mansour, Alejandro Cohen, David H. Heeley, Donna Jackman

Research output: Contribution to journalArticlepeer-review

13 Citations (Scopus)

Abstract

Vitellogenin (VTG) is a protein produced by the liver of oviparous animals. It is being used as a biomarker for exposure to endocrine disruptors in many species. Rainbow trout Vtg has recently been sequenced by the conventional cDNA nucleotide approach. We focused on protein characterization of the intact protein and its derived tryptic and cyanogen bromide peptides by matrix-assisted laser desorption/ionisation and electrospray ionisation mass spectrometry. The molecular mass of the intact protein was found to be 183127 Da. A large number of unidentified peptide ions encourage further structural analysis to propose possible sequence variants and post-translational modifications.

Original languageEnglish
Pages (from-to)509-524
Number of pages16
JournalEuropean Journal of Mass Spectrometry
Volume9
Issue number5
DOIs
Publication statusPublished - 2003
Externally publishedYes

ASJC Scopus Subject Areas

  • Atomic and Molecular Physics, and Optics
  • Spectroscopy

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