Inhibition of [3H] mebendazole binding to tubulin by structurally diverse microtubule inhibitors which interact at the colchicine binding site.

Russell G.J. and Lacey E.

Biochemistry and Molecular Biology International, 1995, 35, 1153-1159.

Publication Date: May 1, 1995


A rapid and convenient radioligand assay was used to characterise the interaction of several structurally diverse microtubule inhibitors with the colchicine binding domain of tubulin. Values determined for the inhibition of [3H]mebendazole binding to tubulin by colchicine, combretastatin A4, NSC 181928, NSC 321567, podophyllotoxin and tubulozole-C provided an independent measure of the relative potency of these compounds. This methodology has several advantages over the inhibition of [3H]colchicine binding as a technique for investigating the molecular mechanisms involved in determining tubulin-ligand interactions.


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