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Lectin probes of glycoconjugates in human salivary glands: 1
Author(s) -
Tolson N. D.,
Daley T. D.,
Wysocki G. P.
Publication year - 1985
Publication title -
journal of oral pathology and medicine
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.887
H-Index - 83
eISSN - 1600-0714
pISSN - 0904-2512
DOI - 10.1111/j.1600-0714.1985.tb00525.x
Subject(s) - glycoconjugate , saliva , myoepithelial cell , lectin , glycoprotein , salivary gland , serous fluid , fucose , biochemistry , chemistry , biology , mannose , carbohydrate , mucin , microbiology and biotechnology , immunohistochemistry , immunology
Research into the oligosaccharide content of glycoproteins in saliva indicates that serous saliva primarily contains N‐glycosidically linked carbohydrate chains with high concentrations of mannose. Where as mucous saliva contains a predominance of O‐glycosidically linked carbohydrate chains with high concentrations of terminal fucose and N‐acetylneuraminic acid molecules. These differences between serous and mucous saliva can be visualized morphologically in salivary gland tissues by differential lectin binding in acinar cells and duct contents. This study utilises a fluorescein‐labelled lectin‐binding method to demonstrate these differences and to study the characteristics of ductal and myoepithelial cells in salivary gland tissues. The results generally confirm the predictable differential binding.