Journal
RAPID COMMUNICATIONS IN MASS SPECTROMETRY
Volume 24, Issue 7, Pages 965-972Publisher
WILEY
DOI: 10.1002/rcm.4474
Keywords
-
Funding
- National Institute of General Medical Sciences, U.S. Department of Health and Human Services [DBI-0642897, GM24349]
- Indiana 21st Century Research and Technology
- Indiana Genomics Initiative (INGEN)
- Lilly Endowment, Inc.
- NIH-National Center for Research Resources (NCRR) [RR018942-02]
- NATIONAL CENTER FOR RESEARCH RESOURCES [P41RR018942] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM024349] Funding Source: NIH RePORTER
Ask authors/readers for more resources
Glycosylation is one of the most common posttranslational modifications (PTMs) of proteins, the characterization of which is commonly achieved through proteomic protocol, involving trypsin digestion followed by liquid chromatography/tandem mass spectrometry (LC/MS/MS). However, it is often not possible to characterize all glycopeptides in a complex sample because of the high complexity of glycoproteomic samples, and the relative lower abundances of glycopeptides in comparison to the unmodified peptides. We present here a targeted MS/MS analysis approach, which utilizes a previously developed computational tool, GlyPID, to guide multiple experiments, thus permitting a complete characterization of all N-glycosylation sites of glycoproteins present in a complex sample. We have tested our approach using model glycoproteins analyzed by high-resolution LTQ-FT MS. The results demonstrate a potential use of our method for a high-throughput characterization of complex mixtures of glycosylated proteins. Copyright (C) 2010 John Wiley & Sons, Ltd.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available