Ochiai H, Schwarz H, Merkl R, Wagle G, Gerisch G
Cell Differ. 1982 Jan;11(1):1-13. doi: 10.1016/0045-6039(82)90011-2.
Monoclonal antibodies against a glycoprotein presumably involved in adhesion of aggregating Dictyostelium discoideum cells have been used for labeling of the antigen at the cell surface. The antigen is distributed over the whole surface of the cells, apparently in form of small clusters. The antigen appears concomitantly with the acquisition of EDTA-stable adhesiveness typical of aggregation competent cells. In contrast, discoidin I, a lectin whose accumulation during development parallels EDTA-stable adhesiveness in another strain (NC-4), is present in nearly the same amounts of growth phase and aggregating cells of AX2-214, the strain used by use. Thus, no correlation exists in this strain between the expression of discoidin I and the development of cell adhesiveness. The 80 kilodalton glycoprotein typical of aggregation competent cells has been purified by affinity chromatography on a monoclonal antibody column. The purified antigen absorbs adhesion-blocking Fab from rabbits. Another antigen strongly reacting with the same monoclonal antibodies has an apparent molecular weight of 106 000 and is not detectable before slugs are formed.
针对一种可能参与盘基网柄菌聚集细胞黏附的糖蛋白的单克隆抗体，已被用于标记细胞表面的抗原。该抗原分布在细胞的整个表面，显然呈小簇状。抗原与获得聚集能力细胞特有的EDTA稳定黏附性同时出现。相比之下，盘基网柄菌凝集素I在发育过程中的积累与另一菌株（NC-4）中EDTA稳定黏附性的变化平行，而在我们使用的AX2-214菌株的生长阶段细胞和聚集细胞中，其含量几乎相同。因此，在该菌株中，盘基网柄菌凝集素I的表达与细胞黏附性的发展之间不存在相关性。具有聚集能力的细胞特有的80千道尔顿糖蛋白已通过在单克隆抗体柱上进行亲和层析纯化。纯化的抗原能从兔血清中吸收黏附阻断性Fab。另一种与相同单克隆抗体强烈反应的抗原，其表观分子量为106000，在蛞蝓形成之前无法检测到。
