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1. an enzyme of the hydrolase class that catalyzes the cleavage of glucosidic linkages between a sialic acid residue and a hexose or hexosamine residue at the nonreducing terminal of oligosaccharides in glycoproteins, glycolipids, and proteoglycans. Deficiency of it is an autosomal recessive trait and is seen in sialidosis and galactosialidosis.
An enzyme that catalyzes the hydrolysis of terminal acetylneuraminic residues from oligosaccharides, glycoproteins, or glycolipids; present on the surface antigen in myxoviruses; used in histochemistry to selectively remove sialomucins, as from bronchial mucous glands and the small intestine; a deficiency of this enzyme produces sialidosis.
neuraminidase(no͝or′ə-mĭn′ĭ-dās′, -dāz′, nyo͝or′-)
A hydrolytic enzyme that removes sialic acid from glycoproteins and is found in many cells and viruses. It occurs on the surface of influenza viruses and enables the release of newly replicated viruses from infected cells.