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

Sugar specific lectins (PNA, RCA I, LPA, SBA, DBA, GSA IB4, GSA II, WGA, LTA, UEA I, Con A, LCA) with and without prior selective glycosidase digestion (sialidase, alpha-fucosidase, alpha-mannosidase, beta-N-acetylglucosaminidase, alpha- and beta-galactosidase, beta-glucosidase) were used in order to investigate the distribution of native accessible carbohydrates and obtain information dealing with the composition of terminal disaccharides within glycoconjugates present in acinar compartments and ductal segments of mammalian (mouse, rat, hare, and rabbit) parotid glands. Glycoconjugates containing variable amounts of mannose, glucose, N-acetylgalactosamine and N-acetylglucosamine were present in the parotid glands of all species. However, these carbohydrate chains exhibited a different composition of terminal sequences within each type of gland. For example, sialylated components having the terminal dimers sialic acid-galactose and sialic acid-N-acetylgalactosamine were found in all acinar cells, whereas fucoglycoconjugates with terminal disaccharide fucose-galactose were localized in the rat striated ducts and hare acinar cells. The terminal sequence alpha-galactose-beta-galactose was demonstrated in the mouse acinar cells. Finally, glycoconjugates characterized by the terminal dimer beta-galactose-N-acetylgalactosamine were demonstrated in the mouse acinar and ductal cells and the rat ductal ones. Thus, present findings outlined and further confirmed the possibility to elucidate the oligosaccharide structure in situ using lectin histochemistry combined with enzymatic degradation.
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PMID:Glycoconjugate composition of mammalian parotid glands elucidated in situ by lectins and glycosidases. 137 7

The N-linked oligosaccharides that were released by hydrazinolysis from glycoproteins of zonae pellucidae of bovine ovarian eggs, were composed of neutral (23%) and acidic (77%) carbohydrate chains; almost all the acidic chains were neutralized by sialidase digestion. Sugar mapping analysis of pyridylaminated N-linked chains by reverse-phase and normal-phase HPLC and 500-MHz 1H-NMR spectroscopy revealed that the major neutral chain is a high-mannose-type oligosaccharide and the acidic chains are di-, tri-, and tetra-antennary, fucosylated complex-type chains that have N-acetyllactosamine repeats in the non-reducing regions. The structures of the neutral chain and the core regions of the acidic chains of N-linked oligosaccharides from the zona proteins of fertilized eggs, which were obtained by the in vitro fertilization method, were essentially the same as those of the ovarian egg zonae. The amount, however, of the acidic chains decreased to 32 mol/100 mol in the fertilized egg zonae, which suggests that a sialidase released from the oocyte during fertilization operates on the zona glycoproteins.
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PMID:Structural characterization of the N-linked carbohydrate chains of the zona pellucida glycoproteins from bovine ovarian and fertilized eggs. 884 11