Features - 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
Source E. coli (cloned from Salmonella typhimurium LT2)
Storage 4°C
Properties - Systematic Name: Acylneuraminyl hydrolase (E.C. 3.2.1.18)
- Molecular weight: 41.3 kDa (SDS-PAGE)
- Km (substrate):
- 0.25 mM (4MUNeuAc)
- 1.52 mM (3'-Sialyliactose)
- 2.66 mM (PA-3'-sialyllactose)
- Inhibitors:
- 2-deoxy-2,3-didehydro-N-acetyl-neuraminic acid
- Ki = 0.38 mM
- Optimum pH:
- pH 5.5–7.0 (Tris-maleate buffer)
- pH 5.5–6.0 (potassium phosphate buffer, sodium acetate buffer, Tris-HCl buffer)
Form Solution containing 50 mM potassium phosphate (pH6.8), 0.1 M sodium chloride, and 0.02% sodium azide.
References - Hoyer, L.L. (1992) Mol. Microbiol. 6 873-884.
- Hoyer, L.L. (1991) J. Biochem. 110:462-7.
Definition of Activity One unit is the amount of enzyme required to hydrolyze 1 µmol of 3'-sialyllactose in 1 minute at 37°C, pH 5.5.
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