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Inhibition of tubulin polymerization by Mebendazole
Authors:J.P. Laclette  G. Guerra  C. Zetina
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
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.
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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