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Arch Oral Biol. 1990;35(2):127-36.

Immunochemistry of high molecular-weight human salivary mucin.

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Department of Oral Biology, State University of New York, Buffalo 14214.


The purpose of this study was to determine the distribution of mucin glycoprotein 1 (MG1) within submandibular, parotid, labial and palatine salivary tissues. Formalin-fixed and frozen tissue sections were examined histochemically with PAS, Alcian blue and Meyer's mucicarmine, and immunocytochemically with an anti-mucin glycoprotein 1 monoclonal antibody (clone 3/E8). Clone 3/E8 was produced in Balb/c mice using mucin-enriched chromatographic fractions from submandibular-sublingual saliva. The monospecificity of 3/E8 was confirmed by immuno-dot blotting and SDS-PAGE/electrophoretic transfer. Clone 3/E8 (IgG1; kappa) was of moderate affinity, and was directed to a carbohydrate-containing, TPCK-trypsin-insensitive and pronase-insensitive epitope on this mucin, which was not blood-group specific. The location of mucin glycoprotein 1 was determined by both indirect (peroxidase-antiperoxidase) and direct methods. Mucin glycoprotein 1 was localized within all labial acini examined, but was not found within parotid tissues. Histochemical methods stained all submandibular, palatine and labial acini, but immunocytochemistry with monoclonal antibody revealed heterogeneous staining with clone 3/E8 in submandibular and palatine tissues. These findings suggest the presence of mucin glycoprotein 1-specific acinar cell subpopulations within human submandibular and palatine salivary tissues.

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