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The α‐Galactose Specificity of Anti‐P k
Author(s) -
Voak D.,
Anstee D.,
Pardoe Grace
Publication year - 1973
Publication title -
vox sanguinis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.68
H-Index - 83
eISSN - 1423-0410
pISSN - 0042-9007
DOI - 10.1111/j.1423-0410.1973.tb04371.x
Subject(s) - galactose , antigen , antibody , trout , chemistry , microbiology and biotechnology , biochemistry , fish <actinopterygii> , biology , stereochemistry , immunology , fishery
. These studies indicate that α‐galactose is the terminal and immunodominant sugar of the P k determinant. Human anti‐P k and the ‘anti‐P k ’ activity of salmon and trout protectins are strongly inhibited by α‐galactosyl groups of galactose, disaccharides and macromolecules, e.g. P 1 substance. Removal of a‐galactose from P 1 substance abolishes its ability to inhibit anti‐P k antibody activity. Anti‐P k antibody has a narrow spectrum for terminal a‐galactosyl groups of cell surface antigens defining those of P k but not those of B, P 1 or P 2 cells, while all these cells are agglutinated by the fish roe protectins. We suggest that anti‐P k antibody selects a larger determinant than the terminal α‐galactosyl group and the full determinant is structurally different from those of B, P 1 and P 2 antigens. By contrast, fish roe agglutinins bind to a part only of the α‐galactosyl group, present in all these antigens.