Glycosylation is important for a number of biological processes and is perhaps the most abundant and complicated of the known post-translational modifications found on proteins. This work combines two-dimensional polyacrylamide gel electrophoresis (2-DE) and lectin blotting to map the salivary glycome, and mass spectrometry to identity the proteins that are associated with the glycome map. A panel of 15 lectins that recognize six sugar-specific categories was used to visualize the type and extent of glycosylation in saliva from two healthy male individuals.
View Article and Find Full Text PDFThe outermost cell envelope structure of many archaea and bacteria contains a proteinaceous lattice termed the surface layer or S-layer. It is typically composed of only one or two abundant, often posttranslationally modified proteins that self-assemble to form the highly organized arrays. Surprisingly, over 100 proteins were annotated to be S-layer components in the archaeal species Methanosarcina acetivorans C2A and Methanosarcina mazei Gö1, reflecting limitations of current predictions.
View Article and Find Full Text PDFA diagnostic test is particularly beneficial if it reveals the level of susceptibility prior to onset of a disease process. In the case of childhood caries, such a diagnostic test affords the opportunity for preventive measures to be implemented before caries begins. Salivary glycoproteins contain a wealth of individually specific oligosaccharide motifs.
View Article and Find Full Text PDFA new saliva test for caries risk assessment introduced in this study integrates a variety of host factors to predict for children, individual risk levels that are tooth-group specific. These various host factors correlate with caries history, DFT (decayed and filled teeth) or DFS (decayed and filled surfaces) in young adults. The test is based on the pattern of genetically determined oligosaccharides present on salivary glycoproteins.
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