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doi:10.1016/1044-0305(92)80003-4    
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Copyright © 1992 Published by Elsevier Science B.V. All rights reserved.

The determination of glycopeptides by liquid chromatography/mass spectrometry with collision-induced dissociation

James J. Conboy and Jack D. HenionCorresponding Author Contact Information

Drug Testing and Toxicology, New York State College of Veterinary Medicine, Cornell University, Ithaca, New York, USA


Received 31 January 1992; 
revised 19 June 1992; 
accepted 19 June 1992. 
Available online 11 January 2002.

Abstract

Glycopeptides derived from ribonuclease B and ovomucoid have been subjected to collision-induced dissociation (CID) in the second quadrupole of a triple quadrupole mass spectrometer. Doubly charged parent ions gave predictable fragmentation that yielded partial sequence information of the attached oligosaccharide as Hex and HexNAc units. Common oxonium ions are observed in the product ion mass spectra of the glycopeptides that correspond to HexNAc+ (m/z 204) and HexHexNAc+ (m/z 366). A strategy for locating the glycopeptides in the proteolytic digest mixtures of glycoproteins by ions spray liquid chromatography mass spectrometry (LC/MS) is described by utilizing CID in the declustering region of the atmospheric pressure ionization mass spectrometer to produce these characteristic oxonium ions. This LC/CID/MS approach is used to identify glycopeptides in proteolytic digest mixtures of ovomucoid, asialofetuin, and fetuin. LC/CID/MS in the selected ion monitoring mode may be used to identify putative glycopeptides from the proteolytic digest of fetuin.

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