This sialidase has a 260-fold kinetic preference for the α2,3 sialyl linkage. The enzyme efficiently cleaves sialyl groups from glycoproteins and glycolipids. It may not release sialic acid from O-linked oligosaccharides on glycoproteins.
Overview
This sialidase has a 260-fold kinetic preference for the alpha 2,3 sialyl linkage
The enzyme efficiently cleaves sialyl groups from glycoproteins and glycolipids
The enzyme may not release sialic acid from O-linked oligosaccharides on glycoproteins
Hoyer, L.L. et al. Cloning, sequencing and distribution of the Salmonella typhimurium LT2 sialidase gene, nanH, provides evidence for interspecies gene transfer. Mol. Microbiol. 6, 873–884 (1992).
Hoyer, L.L. et al. Purification and properties of cloned Salmonella typhimurium LT2 sialidase with virus-typical kinetic preference for sialyl alpha 2-3 linkages J. Biochem. 110,462–467 (1991).
This sialidase has a 260-fold kinetic preference for the α2,3 sialyl linkage. The enzyme efficiently cleaves sialyl groups from glycoproteins and glycolipids. It may not release sialic acid from O-linked oligosaccharides on glycoproteins.
Overview
This sialidase has a 260-fold kinetic preference for the alpha 2,3 sialyl linkage
The enzyme efficiently cleaves sialyl groups from glycoproteins and glycolipids
The enzyme may not release sialic acid from O-linked oligosaccharides on glycoproteins
Hoyer, L.L. et al. Cloning, sequencing and distribution of the Salmonella typhimurium LT2 sialidase gene, nanH, provides evidence for interspecies gene transfer. Mol. Microbiol. 6, 873–884 (1992).
Hoyer, L.L. et al. Purification and properties of cloned Salmonella typhimurium LT2 sialidase with virus-typical kinetic preference for sialyl alpha 2-3 linkages J. Biochem. 110,462–467 (1991).