sialidase


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sialidase

 [si-al´ĭ-dās]
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.
2. the enzyme with this activity specifically cleaving sialic acid–containing gangliosides; it is deficient in mucolipidosis IV. Called also neuraminidase.

si·al·i·dase

(sī-al'i-dās),
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.
Synonym(s): neuraminidase

si·al·i·dase

(sī-al'i-dās)
An enzyme that cleaves terminal acylneuraminic residues from 2,3-, 2,6-, and 2,8-linkages in oligosaccharides, glycoproteins, or glycolipids; present as a 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 will result in cherry-red-spot myoclonus syndrome (q.v.).
References in periodicals archive ?
Requirement of Enhanced Sialidase Activity by Viruses with Enhanced Binding Avidity for Elution from Erythrocytes
Colazzo et al., "NEU3 sialidase strictly modulates GM3 levels in skeletal myoblasts C2C12 thus favoring their differentiation and protecting them from apoptosis," The Journal of Biological Chemistry, vol.
The sialidase family separates from Sia during degradation of sialoglycoconjugates in lysosomes or endosomes (44).
CathA protects sialidase 1 (also known as Neu1) and [beta]-galactosidase ([beta]-Gal) glycosidases against proteolytic degradation by the composition of the LMC and activates Neu1.
We did not find an R292K substitution, which is associated with resistance to the sialidase inhibitors zanamivir, in the NA proteins of virus studied.
we used TRF with lectin NPs for detection that does not require additional sialidase treatment (removal of the terminal sialic acid).
Sia was isolated and separated from bovine submandibular glands, liberated from the mucin by mild acid or sialidase, on cellulose powder in a butanol-propanol-water phase.
DAS181 is a novel investigational sialidase fusion protein, which removes sialic acid-containing receptors from the surface of respiratory epithelial cells, and thus prevents PIV and influenza virus from binding to these cells [6].