Whole-body extracts of the bivalve Anodonta anatina gave apparent
non-specific agglutination with enzyme treated human erythrocytes, but a decreasing
gradient of agglutination became evident of the order 0I, BI, A(2)BI, A(2)I, (A(3)I, A(x)I,
O(h)l), A(1)BI, A(1)I, adult ii, cord ii cells, suggesting an anti-I specificity.
The agglutinin was inhibited by galactose and its oligosaccharides, particularly
lactose and stachyose.
Absorption tests with different red cell types, inhibition tests with salivas and
simple sugars, and the effect of different cations, suggested the presence of additional
agglutinins in the extract.