ANTIBODY‐COMBINING OLIGOSACCHARIDES FROM A CHICK ALLANTOIC GLYCOPEPTIDE SULPHATE ASSOCIATED WITH INFLUENZA VIRUS HAEMAGGLUTININ

Publisher Website
Google Scholar
Abstract
Oligosaccharides that combine with antibody to a chick allantoic glycopeptide sulphate have been produced both by dilute acid and alkali treatment of the glycopeptide. Chemical and immunological assays of the oligosaccharides in conjunction with periodate oxidation studies and enzyme treatments have helped to elucidate the carbohydrate residues responsible for antibody‐combining activity in the parent glycopeptide. Peptide, sialic acid, 2‐amino‐2‐deoxyglucose and 2‐amino‐2‐deoxygalactose residues in the glycopeptide play no part in conferring activity, but D‐galactose and, to a lesser extent, fucose are sole components of the active site. Two types of D)‐galactose determinant residues are present, differing in their susceptibility to periodate exidation.