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Anal Chem. 2010 Dec 15;82(24):10095-101. doi: 10.1021/ac1020722. Epub 2010 Nov 15.

Improved mass spectrometric characterization of protein glycosylation reveals unusual glycosylation of maize-derived bovine trypsin.

Author information

1
Department of Chemistry, Washington University in St. Louis, St. Louis, Missouri 63130, United States.

Abstract

Although bottom-up proteomics using tryptic digests is widely used to locate post-translational modifications (PTM) in proteins, there are cases where the protein has several potential modification sites within a tryptic fragment and MS(2) strategies fail to pinpoint the location. We report here a method using two proteolytic enzymes, trypsin and pepsin, in combination followed by tandem mass spectrometric analysis to provide fragments that allow one to locate the modification sites. We used this strategy to find a glycosylation site on bovine trypsin expressed in maize (TrypZean). Several glycans are present, and all are attached to a nonconsensus N-glycosylation site on the protein.

PMID:
21077632
PMCID:
PMC3005374
DOI:
10.1021/ac1020722
[Indexed for MEDLINE]
Free PMC Article

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