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Comparison of Glycopeptide Fragmentation by Collision Induced Dissociation and Ultraviolet Photodissociation.


ABSTRACT: A comparison of the fragmentation pathways of both protonated and deprotonated O-linked glycopeptides from fetuin and ?-casein obtained upon collision induced dissociation (CID) and 193 nm ultraviolet photodissociation (UVPD) in a linear ion trap is presented. A strategy using non-specific pronase digestion, zwitterionic hydrophilic interaction liquid chromatography (ZIC-HILIC) solid phase extraction (SPE) enrichment, and nano-liquid chromatography (nano-LC) is employed. UVPD of deprotonated glycopeptides generally produced the greatest array of fragment ions, thus affording the most diagnostic information about both glycan structure and peptide sequence. In addition, UVPD generated unique fragment ion such as Y-type ions arising from cleavage at the N-terminus of proline. CID and UVPD of protonated glycopeptides produced fragment ions solely from glycan cleavages.

SUBMITTER: Ko BJ 

PROVIDER: S-EPMC4379704 | biostudies-literature | 2015 Feb

REPOSITORIES: biostudies-literature

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Comparison of Glycopeptide Fragmentation by Collision Induced Dissociation and Ultraviolet Photodissociation.

Ko Byoung Joon BJ   Brodbelt Jennifer S JS  

International journal of mass spectrometry 20150201 1


A comparison of the fragmentation pathways of both protonated and deprotonated O-linked glycopeptides from fetuin and κ-casein obtained upon collision induced dissociation (CID) and 193 nm ultraviolet photodissociation (UVPD) in a linear ion trap is presented. A strategy using non-specific pronase digestion, zwitterionic hydrophilic interaction liquid chromatography (ZIC-HILIC) solid phase extraction (SPE) enrichment, and nano-liquid chromatography (nano-LC) is employed. UVPD of deprotonated gly  ...[more]

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