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Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry
- Source :
- Journal of proteome research. 5(6)
- Publication Year :
- 2006
-
Abstract
- Glycoproteins make up a major and important part of the salivary proteome and play a vital role in maintaining the health of the oral cavity. Because changes in the physiological state of a person are reflected as changes in the glycoproteome composition, mapping the salivary glycoproteome will provide insights into various processes in the body. Salivary glycoproteins were identified by the hydrazide coupling and release method. In this approach, glycoproteins were coupled onto a hydrazide resin, the proteins were then digested and formerly N-glycosylated peptides were selectively released with the enzyme PNGase F and analyzed by LC-MS/MS. Employing this method, coupled with in-solution isoelectric focusing separation as an additional means for pre-fractionation, we identified 84 formerly N-glycosylated peptides from 45 unique N-glycoproteins. Of these, 16 glycoproteins have not been reported previously in saliva. In addition, we identified 44 new sites of N-linked glycosylation on the proteins.
- Subjects :
- chemistry.chemical_classification
PNGase F
Proteomics
Saliva
Two-dimensional gel electrophoresis
Glycosylation
Isoelectric focusing
Molecular Sequence Data
General Chemistry
Tandem mass spectrometry
Biochemistry
Mass Spectrometry
chemistry.chemical_compound
chemistry
Humans
Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
Electrophoresis, Gel, Two-Dimensional
Amino Acid Sequence
Glycoprotein
Glycoproteins
Subjects
Details
- ISSN :
- 15353893
- Volume :
- 5
- Issue :
- 6
- Database :
- OpenAIRE
- Journal :
- Journal of proteome research
- Accession number :
- edsair.doi.dedup.....bf6b5a35d7307822ce7bc77c1edb3861