Binding of maytansine to tubulin: competition with other mitotic inhibitors.
The effect of maytansine on the binding of [3H]vinblastine and [3H]colchicine to tubulin was examined by Sephadex gel filtration column chromatography. When varying concentrations of maytansine were employed, competition between vinblastine and maytansine was observed at a vinblastine to maytansine ratio of 1:10 and 1:100, while a colchicine to maytansine ratio of 1:100 did not affect the binding of colchicine to tubulin. These results confirm earlier findings with a DEAE-cellulose disc paper assay and a tubulin polymerization assay that maytansine shares a common binding site with vinblastine and support the view that tubulin has at least two drug binding sites.
D000818:Animals; D001667:Binding, Competitive; D003078:Colchicine / Q000378:metabolism*; D008453:Maytansine / Q000378:metabolism*; D008938:Mitosis / Q000187:drug effects*; D010078:Oxazines / Q000378:metabolism*; D013552:Swine; D014404:Tubulin / Q000378:metabolism*; D014747:Vinblastine / Q000378:metabolism*
D010078:Oxazines; D014404:Tubulin; D008453:Maytansine; D014747:Vinblastine; D003078:Colchicine