Amanai Kazuhito, Sakai Mie, Sakurai Sho, Mori Toshio, Nikaido Osamu, Ohtaki Tetsuya
Department of Biology, Faculty of Science, Kanazawa University, Kanazawa 920, Japan.
Division of Radiation Biology, Faculty of Pharmaceutical Science, Kanazawa University, Kanazawa 920, Japan.
Dev Growth Differ. 1991 Aug;33(4):421-427. doi: 10.1111/j.1440-169X.1991.421_a.x.
Monoclonal antibodies were prepared against the 350 kDa lectin purified from larval hemolymph of the silkworm, Bombyx mori. The antibodies inhibited the hemagglutinating activity (HA activity) and bound specifically to the hemolymph 350 kDa lectin on Western blotting analysis. Immunohistological observations revealed the occurrence of lectin in the cuticular intima of the anterior silk gland, but not the middle or posterior silk glands of fifth instar larvae of Bombyx mori. Extracts from the anterior silk glands showed HA activity and exhibited the same biochemical characteristics as those of the 350 kDa lectin in the hemolymph. These results suggested that lectin-like molecules in epithelial tissues may be important in histolysis during molting and metamorphosis.
制备了针对从家蚕幼虫血淋巴中纯化的350 kDa凝集素的单克隆抗体。这些抗体抑制了血凝活性(HA活性),并且在蛋白质印迹分析中与血淋巴350 kDa凝集素特异性结合。免疫组织学观察显示,凝集素存在于家蚕五龄幼虫前丝腺的表皮内膜中,而中丝腺和后丝腺中则没有。前丝腺提取物显示出HA活性,并且表现出与血淋巴中350 kDa凝集素相同的生化特性。这些结果表明,上皮组织中的凝集素样分子可能在蜕皮和变态过程中的组织溶解中起重要作用。