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Your search keyword '"Ray, Kevin B."' showing total 2 results
Start Over Author "Ray, Kevin B." Topic glycosylation
2 results on '"Ray, Kevin B."'

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

Author

Zhang H, Huang RY, Jalili PR, Irungu JW, Nicol GR, Ray KB, Rohrs HW, and Gross ML

Subjects
Animals, Cattle, Pepsin A metabolism, Protein Processing, Post-Translational, Proteomics methods, Trypsin analysis, Glycosylation, Peptide Fragments analysis, Tandem Mass Spectrometry methods, Trypsin metabolism, Zea mays metabolism
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.

Published
2010
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2. Improved Mass Spectrometric Characterization of Protein Glycosylation Reveals Unusual Glycosylation of Maize-Derived Bovine Trypsin.

Author

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

Subjects
*POST-translational modification, *PROTEINS, *PANCREATIC secretions, *ENZYMES, *TRYPSIN, *PEPSIN, *GLYCOSYLATION, *GENETIC translation
Abstract

Although bottom-up proteomics using tryplic 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 noncon-sensus N-glycosylation site on the protein. [ABSTRACT FROM AUTHOR]

Published
2010
Full Text
View/download PDF

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