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A Novel Strategy for Characterization of Glycosylated Proteins Separated by Gel Electrophoresis.

Publikation: KonferencebidragKonferenceabstrakt til konferenceForskning

  • Martin Larsen
  • Peter Durand Skottrup
  • Jan Johannes Enghild
  • Peter Højrup
  • Peter Roepstorff
Protein glycosylation can be vital for changing the function or physiochemical properties of a protein. Abnormal glycosylation can lead to protein malfunction, resulting in severe diseases. Therefore, it is important to develop techniques for characterization of such modifications in proteins at a sensitivity level comparable with state-of-the-art proteomics. Whereas techniques exist for characterization of high abundant glycoproteins, no single method is presently capable of providing information on both site occupancy and glycan structure on a single band or spot excised from an electrophoretic gel. We present a new technique, which allows full characterization of low amounts of glycoproteins separated by gel electrophoresis. The method takes advantage of sequential specific and non-specific enzymatic treatment, followed by selective purification and characterization of the glycopeptides using graphite powder micro-columns in combination with mass spectrometry. The method is faster and more sensitive than previous approaches and would be ideal for proteomics studies and verification of correct glycosylation of recombinant glycoproteins.
OriginalsprogEngelsk
Publikationsdato2004
Antal sider1
StatusUdgivet - 2004
Eksternt udgivetJa
Begivenhed52nd ASMS Conference on Mass Spectrometry and Allied Topics - Nashville, USA
Varighed: 23 maj 200427 maj 2004

Konference

Konference52nd ASMS Conference on Mass Spectrometry and Allied Topics
LandUSA
ByNashville
Periode23/05/200427/05/2004

Bibliografisk note

FASEB JOURNAL ; 18 (8), p. C153-C153 Suppl

ID: 33227772