Neuraminidase can block attachment of type 3 reovirus to cell membranes. This effect is related to the ability of neuraminidase to hydrolysis sialic acid residues within cell surface receptors. Neuraminidase cleavage of sialic acid groups has been used to study recognition by antibodies of glycoprotein structures. The use of neuraminidase in the estimation of N-acetylneuraminic acid was compared favorably to two other methods. Neuraminidases are used to cleave terminal N-acetyl neuraminic acid (sialic acid) from a variety of glycoproteins. The enzyme from Clostridium perfringens cleaves terminal sialic acid residues which are α-2,3- α-2,6- or α-2,8-ed to Gal, GlcNac, GalNAc, AcNeu, GlcNeu, oligosaccharides, glycolipids or glycoproteins. The relative rate of cleavage decreases in the order: α-2-3 > α-2-6 . α-2-8. Neuraminidase from C. perfringens cleaves α-2-3 ed sialic acid residues most efficiently, compared to A. ureafaciens, (Sigma N3642) which preferentially cleaves α-2-6 ed residues. The use of neuraminidase to remove sialic acid residues from glycoproteins on cell surfaces has been frequently reported. Generally, procedures have indicated using neuraminidase in PBS at 37°C for 30 minutes, followed by several washings with PBS. Treatment of tissue sections with neuraminidase at much lower concentrations require longer incubation: for 1-4 U/mL in 0.1 M acetate buffer pH 4.2-5, from 2 to 20 hours at 37 °C. | 
