[No authors listed]
A carbohydrate-binding protein assayed by its ability to agglutinate formalinized sheep erythrocytes is synthesized between 3 and 9 hr after Dictyostelium discoideum cells are deprived of food, as the cells become cohesive. Agglutination of erythrocytes by this protein was inhibited by N-acetyl-D-galactosamine, D-galactose, and L-fucose, but other monosaccharides had little or no effect. The protein bound completely to Sepharose 4B, and was isolated in highly purified form by elution with D-galactose. It appears to be present on the surface of cohesive but not vegetative slime-mold cells. The possibility that this protein may mediate intercellular adhesion in Dictyostelium is considered.
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