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THE SIGNIFICANCE OF NEURAMINIC ACID, SERINE AND THREONINE FOR A GLYCOPROTEIN INHIBITING INFLUENZA VIRUS HAEMAGGLUTINATION
Author(s) -
Gottschalk Alfred
Publication year - 1965
Publication title -
australian journal of experimental biology and medical science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.999
H-Index - 104
eISSN - 1440-1711
pISSN - 0004-945X
DOI - 10.1038/icb.1965.72
Subject(s) - neuraminic acid , threonine , neuraminidase , glycoprotein , serine , chemistry , biochemistry , residue (chemistry) , virus , virology , glycosidic bond , stereochemistry , enzyme , biology
Summary A short review is given of the impact which Sir Macfarlane Burnet's observations, on the influenza virus enzyme and RDE and on the influenza virus haemagglutinin inhibitors, has had on the development of the chemistry of glycoproteins in general and on the elucidation of the molecular structure of neuraminic acid in particular. The structure of the ovine submaxillary (OSM) glycoprotein, prepared from sheep submaxillary glands, is described and its potency as influenza virus haemagglutinin inhibitor discussed in terms of multiple carbohydrate groups, each terminated by a neuraminic acid residue. Evidence is presented that in OSM (from three‐year‐old sheep) the predominant linkage of carbohydrate to protein is an O‐glycosidic linkage to the hydroxyl group of serine and threonine residues. This linkage is easily split by dilute alkali, most probably by the mechanism of ß‐elimination.