Glycosylation is important for a number of biological processes and is the most common and among the most complicated post-translational modification found on proteins. Therefore it is not surprising that changes in the glycoform population have been linked to many diseases including cancer, atherosclerosis, rheumatoid arthritis, pre-term labor and caries risk to name a few (1-4). By understanding the glycosylation profile in both healthy and diseased individuals, we hope to detect markers that can be used for diagnosing and monitoring the progression of disease. Lectins are a class of proteins that recognize a wide variety of specific oligosaccharide motifs. This work combines two-dimensional gel electrophoresis, lectin blotting, and mass spectrometry to map the salivary glycome.
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