Purification and comparison of two developmentally regulated lectins from Dictyostelium discoideum. Discoidin I and II.
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.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002454:Cell Differentiation; D002846:Chromatography, Affinity; D004023:Dictyostelium / Q000032:analysis* / Q000378:metabolism; D004912:Erythrocytes / Q000276:immunology; D006386:Hemagglutination Tests; D037102:Lectins / Q000032:analysis* / Q000302:isolation & purification / Q000378:metabolism; D008970:Molecular Weight; D009235:Myxomycetes / Q000032:analysis*; D010446:Peptide Fragments / Q000032:analysis; D011817:Rabbits / Q000276:immunology
D000596:Amino Acids; D037102:Lectins; D010446:Peptide Fragments