Rosen S D, Kafka J A, Simpson D L, Barondes S H
Proc Natl Acad Sci U S A. 1973 Sep;70(9):2554-7. doi: 10.1073/pnas.70.9.2554.
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.
一种通过其凝集甲醛固定的绵羊红细胞的能力来检测的碳水化合物结合蛋白，是在盘基网柄菌细胞被剥夺食物后3至9小时之间合成的，此时细胞变得具有粘性。该蛋白对红细胞的凝集作用受到N-乙酰-D-半乳糖胺、D-半乳糖和L-岩藻糖的抑制，但其他单糖几乎没有影响。该蛋白能完全结合到琼脂糖4B上，并通过用D-半乳糖洗脱以高度纯化的形式分离出来。它似乎存在于具有粘性的而非营养性的黏菌细胞表面。人们考虑了这种蛋白可能介导盘基网柄菌细胞间黏附的可能性。
