Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.1.53 (sialidase)
 2,694 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Structures of oligosaccharides in submandibular glycoproteins were evaluated in situ. Sections of fixed paraffin-embedded glands from rats, mice, hamsters, sheep, and man were stained with a battery of lectins conjugated to horseradish peroxidase in conjunction with other methods, such as digestion with sialidase with or without prior saponification and/or periodate oxidation. Secretory glycoproteins showed a characteristic lectin binding pattern for each genus. Sialoglycoconjugates were detected in acinar cell secretions in all genera except the rat but differed with respect to the linkage of sialic acid to penultimate beta-galactose or alpha-N-acetylgalactosamine. Species and strains of mice showed minor differences in the structure of secretory glycoproteins. Sexes differed similarly in some but not other mouse species. Individual differences were seen in human glands, where oligosaccharide structure varied in relation to ABO blood group. In some species, heterogeneity in glycoprotein structure was observed among morphologically similar cells within a gland. Differences in the structure of salivary secretions between genera and between humans of different ABO blood type and secretor status substantiate biochemical and histochemical findings. The results showing species, sex, and individual differences in mice and heterogeneity in acinar cells in several species suggest a greater degree of genetic and perhaps hormonal influence on the synthesis of salivary glycoproteins than has previously been recognized.
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PMID:Genetic and sex-related differences in the structure of submandibular glycoconjugates. 244 18