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Eur. J. Mass Spectrom. DOI: 10.1255/ejms.572

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 Q time-of-flight mass spectrometry

Joseph Banoub,a,b* Pierre Thibault,c Alejandro Cohen,b Atef Mansour,a David H. Heeleyb and Donna Jackmanb
aDepartment of Fisheries and Oceans Canada, Science, Oceans and Environment Branch, St John's, PO Box 5667, Newfoundland A1C 5X1, Canada
bDepartment of Biochemistry, Memorial University of Newfoundland, St John's, Newfoundland A1C 5S7, Canada
cProtein Analysis, Caprion Pharmaceuticals, 7150 Alexander Fleming, Montreal, Quebec H4S 2C8, Canada

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 conventional cDNA nucleotide approach. We focused on protein characterisation of the intact protein and its derived tryptic and cyanogen bromide peptides by matrix-assisted laser desorption/ionisation and electrospray ionization 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.

Keywords: vitellogenin, characterization, cyanogen bromide, tryptic, MALDI MS, ESI MS, fingerprint


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