Rösner H, Schönharting M
Hoppe Seylers Z Physiol Chem. 1977 Jul;358(7):915-9.
The binding of the alkaloid colchicine and its metabolite colchiceine to different membranes and gangliosides has been investigated. In contrast to colchicine, colchiceine binds to erythrocyte ghosts, plasma membranes of rat liver and heart muscle, and synaptosomes of rat brain. The binding properties of isolated gangliosides are analogous to those of the membranes investigated. On a molar basis the binding capacities of the gangliosides GT1, GD1a and GM1 for colchiceine are 7:4:1, respectively. The binding of alkaloid to ganglioside structures is diminished in the presence of EDTA and after pretreatment with neuraminidase, suggesting a specific, Ca2 -dependent interaction of colchiceine with gangliosides. The results are discussed with respect to the different biological activities of colchicine and its metabolite colchiceine.
已对生物碱秋水仙碱及其代谢产物秋水仙酰胺与不同膜及神经节苷脂的结合情况进行了研究。与秋水仙碱不同，秋水仙酰胺能与红细胞血影、大鼠肝脏和心肌的质膜以及大鼠脑突触体结合。分离出的神经节苷脂的结合特性与所研究的膜类似。以摩尔计，神经节苷脂GT1、GD1a和GM1对秋水仙酰胺的结合能力分别为7:4:1。在存在乙二胺四乙酸（EDTA）的情况下以及用神经氨酸酶预处理后，生物碱与神经节苷脂结构的结合会减弱，这表明秋水仙酰胺与神经节苷脂存在特异性的、依赖钙离子的相互作用。结合秋水仙碱及其代谢产物秋水仙酰胺的不同生物活性对结果进行了讨论。
