These studies indicate that α-galactose is the terminal and immunodominant sugar of the Pk 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 α-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 α-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.
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