Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry.

Article Details


Ramachandran P, Boontheung P, Xie Y, Sondej M, Wong DT, Loo JA

Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry.

J Proteome Res. 2006 Jun;5(6):1493-503.

PubMed ID
16740002 [ View in PubMed

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.

DrugBank Data that Cites this Article

NameUniProt ID
Alpha-1-acid glycoprotein 1P02763Details
Neutrophil gelatinase-associated lipocalinP80188Details
Alpha-amylase 1P04745Details
Beta-2-glycoprotein 1P02749Details
Carcinoembryonic antigen-related cell adhesion molecule 5P06731Details
Ig alpha-2 chain C regionP01877Details
Complement C4-BP0C0L5Details
Leucine-rich alpha-2-glycoproteinP02750Details
Immunoglobulin J chainP01591Details