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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/neu·ra·min·i·dase/ (-ah-min´ĭ-dās) an enzyme of the surface coat of myxoviruses that destroys the neuraminic acid of the cell surface during attachment, thereby preventing hemagglutination.
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.
an enzyme that catalyzes the cleavage of N-acetyl neuraminic acid from mucopolysaccharides. A hereditary deficiency of the enzyme causes sialidosis and is associated with galactogialidosis; it is characterized by mental retardation and skeletal changes, especially dysotosis multiplex. Also called sialidase. See also sialidosis.
1. an enzyme that cleaves the terminal N-acetylneuraminic acid from mucoproteins.
2. a structural component occurring as a spike in the envelope of ortho- and paramyxoviruses.