期刊
JOURNAL OF PROTEOME RESEARCH
卷 5, 期 6, 页码 1493-1503出版社
AMER CHEMICAL SOC
DOI: 10.1021/pr050492k
关键词
glycoproteins; tandem mass spectrometry; salivary proteins; 2D gel electrophoresis; mucin; solution isoelectric focusing
资金
- NIDCR NIH HHS [U01 DE016275] Funding Source: Medline
- NIGMS NIH HHS [GM07185] Funding Source: Medline
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 prefractionation, 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.
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