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JBC, Vol. 250, Issue 19, 7714-7721, Oct, 1975

Purification and comparison of two developmentally regulated lectins from Dictyostelium discoideum. Discoidin I and II

W. A. Frazier, S. D. Rosen, R. W. Reitherman and S. H. Barondes

When cells of the cellular slime mold Dictyostelium discoideum differentiate from a nonsocial amoeboid form to a cohesive, aggregating form, they synthesize a lectin-like protein called discoidin, which is present on the cell surface. It is now reported that discoidin consists of two distinct lectins, designated discoidin I and discoidin II, which, although similar in some respects, differ in their electrophoretic mobilities, isoelectric points, subunit molecular weights, amino acid compositions, tryptic peptide maps, the erythrocyte species which they agglutinate, and the sensitivity of their agglutination activity to inhibition by monosaccharides. Furthermore, discoidins I and II differ in their developmental regulation as evidenced by the distinct time courses of their appearance during differentiation.
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