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

Author

Zhang, Hao, Huang, Richard Y-C., Jalili, Pegah R., Irungu, Janet W., Nicol, Gordon R., Ray, Kevin B., Rohrs, Henry W., and Gross, Michael L.

Subjects
Mass spectrometry -- Methods, Proteins -- Chemical properties, Proteins -- Identification and classification, Trypsin -- Chemical properties, Trypsin -- Usage, Corn -- Chemical properties, Corn -- Genetic aspects, Chemistry
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 MS2 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. 10.1021/ac1020722

Published
2010

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