Den H, Chin J H
J Biol Chem. 1981 Aug 10;256(15):8069-73.
Antisera against a beta-D-galactoside-specific lectin purified to homogeneity from embryonic chick thigh muscle and from adult chicken livers were raised in rabbits. The sera contained antibodies which strongly inhibited the hemagglutinin activity of the lectin. Immune and preimmune [125I]IgG and [125I]Fab preparations were tested for ability to bind to monolayers of cultured chick myoblasts and showed no significant differences in binding. Thus, we were unable to detect the lectin on the cell surface. When added to myoblast cultures, the purified lectin had no influence on the process of myoblast fusion. Furthermore, neither anti-lectin IgG nor Fab fragments interfered with myotube formation when present at high concentration in fusing cultures. On the basis of these results, we conclude that intercellular interactions between the lectin and complementary cell surface receptors do not play a role in myoblast adhesion and fusion in vitro.
从胚胎鸡大腿肌肉和成年鸡肝脏中纯化出一种β-D-半乳糖苷特异性凝集素，并将其制备成抗血清注射到兔子体内。这些血清中含有能强烈抑制该凝集素血凝活性的抗体。对免疫和免疫前的[125I]IgG及[125I]Fab制剂进行测试，以检测其与培养的鸡成肌细胞单层结合的能力，结果显示结合能力无显著差异。因此，我们无法在细胞表面检测到该凝集素。将纯化的凝集素添加到成肌细胞培养物中，对成肌细胞融合过程没有影响。此外，当在融合培养物中以高浓度存在时，抗凝集素IgG和Fab片段均不干扰肌管形成。基于这些结果，我们得出结论：凝集素与互补细胞表面受体之间的细胞间相互作用在体外成肌细胞黏附和融合过程中不起作用。
