Structural Features of Newcastle Disease Virus- and Anti-Ovomucin Antibody-Binding Glycopeptides from Pronase-Treated Ovomucin

Pronase-treated ovomucin was applied on a Sephacryl S-400 column chromatography and separated into five fractions. The SDS−polyacrylamide gel electrophoretic pattern, and amino acid and carbohydrate compositions, of each of the obtained fractions were compared to those of ovomucin and its α- and β-subunits. Subsequently, bindings of each fraction to hen newcastle disease virus (NDV) and anti-ovomucin antibodies were estimated. It was found that the P1, P2, and P3 fractions from the β-subunit which were composed of O-glycoproteins, containing more or less clustered sialic acid moieties, had higher binding activity to NDV, while the peptide-rich P4 and P5 fractions mainly derived from the α-subunit had higher binding activity to the anti-ovomucin antibodies.