z-logo
Premium
Studies on the Antigenic Activity of Yeasts
Author(s) -
Suzuki Shigeo,
Sunayama Hiroyoshi,
Saito Takeshi
Publication year - 1968
Publication title -
japanese journal of microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0021-5139
DOI - 10.1111/j.1348-0421.1968.tb00365.x
Subject(s) - mannan , mannose , chemistry , biochemistry , disaccharide , stereochemistry , residue (chemistry) , moiety , antigen , galactose , saccharomyces cerevisiae , polysaccharide , yeast , biology , immunology
In order to determine the determinant antigenic group of the mannan of Saccharomyces cerevisiae , a series of inhibition tests were carried out employing oligosaccharides which separated from the acetolyzate and the hydrolyzate of the mannan. Tetraose, Man α1→3 Man α1→2 Man α→2 Man 2 , corresponding to the structure of the longer branching moieties of the mannan showed the strongest inhibition, while the isomer, Man α1→6 Man α1→6 Man, corresponding to the core moiety, produced only one‐tenth the inhibition of the former. This provides evidence that the branching moieties of the mannan play important role in combining with antibody. The fact that the disaccharide, Man α→3, showed significantly stronger inhibition than those of the other disaccharides, Man α1→2 Man and Man α1→6 Man, indicates that the most important part of the determinant group of the mannan is α1→3 linked D‐mannose residue. The antigenic inactivity of the periodate‐oxidized mannan containing unoxidized mannose residues indicates that the presence of 3‐O‐substituted‐D‐mannose residues adjacent to the D‐mannose residues and joined with α1→d2 linkages, are essential to fit the combining site of the antibody.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here