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N- and O-linked glycosylation site profiling of the human basic salivary proline-rich protein 3M.
- Source :
-
Journal of separation science [J Sep Sci] 2016 May; Vol. 39 (10), pp. 1987-97. Date of Electronic Publication: 2016 Apr 29. - Publication Year :
- 2016
-
Abstract
- In the present study, we show that the heterogeneous mixture of glycoforms of the basic salivary proline-rich protein 3M, encoded by PRB3-M locus, is a major component of the acidic soluble fraction of human whole saliva in the first years of life. Reversed-phase high-performance liquid chromatography with high-resolution electrospray ionization mass spectrometry analysis of the intact proteoforms before and after N-deglycosylation with Peptide-N-Glycosidase F and tandem mass spectrometry sequencing of peptides obtained after Endoproteinase GluC digestion allowed the structural characterization of the peptide backbone and identification of N- and O-glycosylation sites. The heterogeneous mixture of the proteoforms derives from the combination of 8 different neutral and sialylated glycans O-linked to Threonine 50, and 33 different glycans N-linked to Asparagine residues at positions 66, 87, 108, 129, 150, 171, 192, and 213.<br /> (© 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)
Details
- Language :
- English
- ISSN :
- 1615-9314
- Volume :
- 39
- Issue :
- 10
- Database :
- MEDLINE
- Journal :
- Journal of separation science
- Publication Type :
- Academic Journal
- Accession number :
- 26991339
- Full Text :
- https://doi.org/10.1002/jssc.201501306