Neuraminidase (Sialidase) from Arthrobacter ureafaciens Roche

Acylneuraminyl hydrolase
EC 3.2.1.18
Molecular weight: band I M_r = 51 kD, band II M_r = 39 kD (SDS-PAGE)
Optimum pH: 5.0 - 5.5
Specififc activity: approx. 25 U/mg total protein at 25°C (approximately 35 U/mg total protein at 37°C) and pH 5.0 with N-acetyl-neuraminosyl-D-lactose as the substrate.
Specificity: Cleaves terminal sialic-acid residues that are α2,3-, α2,6-, or α2,8-linked to Gal, GlcNAc, GalNAc, AcNeu, GlcNeu, oligosaccharides, glycolipids, or glycoproteins. Relative rate of cleavage is α2→6 >α2→3 >α2→8, determined on bonds in tri- and tetrasaccharides.

Solution in 10 mM sodium phosphate, 0.1% Micr-O-protect,
0.25 mg/ml BSA, pH 7

Contaminants: proteases are not detectable (casein, resorufin-labeled, as the substrate)