Inhibition of tubulin polymerization by Mebendazole |
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Authors: | J.P. Laclette G. Guerra C. Zetina |
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Affiliation: | 1. Departmento de Investigación Clínica; Instituto Nacional de Pediatría DIF; A.P. 101-36, México 22, D.F., México;2. Escuela Nacional de Estudios Profesionales Cuautitlán, U.N.A.M. México 22, D.F., México;3. Departmento de Biología Celular, Centro de Investigación y Estudios Avanzados del IPN México 22, D.F., México |
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Abstract: | 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 per tubulin dimer. This site has an affinity constant of 2.8 × 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. |
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Keywords: | MESv2(n-morpholino) ethane sulfonic acid EGTA Ethylenglycol-bis-(B-amino-ethyl ether) N,N-tetraaetic acid DMSO Dimethyl sulfoxide |
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