INHIBITION OF TUBULIN POLYMERIZATION BY MEBENDAZOLE
INHIBITION OF TUBULIN POLYMERIZATION BY MEBENDAZOLE
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DOI：
10.1016/0006-291x(80)90349-6
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发表时间：
1980-01-01
影响因子：
3.1
通讯作者：
ZETINA, C
中科院分区：
文献类型：
--
作者：
LACLETTE, JP;GUERRA, G;ZETINA, C
本文研究了新型抗蠕虫药甲苯咪唑（甲基-5-苯甲酰基苯并咪唑-2-氨基甲酸酯）与微管蛋白的相互作用。超微和比浊证据表明甲苯咪唑对微管蛋白的体外聚合有抑制作用。Scatchard图分析显示甲苯咪唑/微管蛋白二聚体的单一结合位点。该位点的亲和常数为2.8 × 106。105 M-1。竞争实验表明，该结合位点与秋水仙碱相同，即使两种化合物在化学上不相关。甲苯咪唑被认为是研究微管蛋白组装的有用工具。
The interaction of mebendazole (methyl-5-benzoyl benzimidazole-2-carbamate), a new antihelminthic drug, with tubulin was studied. Ultramicroscopic and turbidimetric evidence shows an inhibitory effect of mebendazole on the in vitro polymerization of tubulin. Scatchard plot analysis shows a single binding site for mebendazole/tubulin dimer. This site has an affinity constant of 2.8 .times. 105 M-1. Competition experiments demonstrate that this binding site is the same as for Colchicine, even when both compounds are not chemically related. Mebendazole is proposed as a useful tool for the study of tubulin assembly.