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ANTIBODY‐COMBINING OLIGOSACCHARIDES FROM A CHICK ALLANTOIC GLYCOPEPTIDE SULPHATE ASSOCIATED WITH INFLUENZA VIRUS HAEMAGGLUTININ
Author(s) -
Higginbotham John D.,
Schöyen Rolf,
MortenssonEgnund Karen,
How Mervyn J.,
Harboe Arild
Publication year - 1971
Publication title -
acta pathologica microbiologica scandinavica section b microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.909
H-Index - 88
eISSN - 1600-0463
pISSN - 0365-5563
DOI - 10.1111/j.1699-0463.1971.tb00072.x
Subject(s) - glycopeptide , fucose , biochemistry , sialic acid , periodate , glycoprotein , antibody , galactose , periodic acid , chemistry , amino acid , peptide , biology , mannose , immunology , antibiotics
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.