Improved mass spectrometric characterization of protein glycosylation reveals unusual glycosylation of maize-derived bovine trypsin.
Anal Chem
; 82(24): 10095-101, 2010 Dec 15.
Article
in En
| MEDLINE
| ID: mdl-21077632
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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Peptide Fragments
/
Glycosylation
/
Trypsin
/
Zea mays
/
Tandem Mass Spectrometry
Limits:
Animals
Language:
En
Journal:
Anal Chem
Year:
2010
Document type:
Article
Affiliation country:
United States