Báo cáo khoa học: Dolastatin 15 binds in the vinca domain of tubulin as demonstrated by Hummel–Dreyer chromatography
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The antimitotic depsipeptide dolastatin 15 was radiolabeledwith tritium in its amino-terminal dolavaline residue.Dolastatin 15, although potently cytotoxic, is a relativelyweak inhibitor oftubulin assembly and does not inhibit thebinding ofany other ligand to tubulin. The only methodo-logy found to demonstrate an interaction between the dep-sipeptide and tubulin was Hummel–Dreyer equilibriumchromatography on Sephadex G-50 superfine. The averageapparent Kd value obtained in these studies was about30lM, with no difference observed when column size ortubulin concentration was varied....
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Báo cáo khoa học: Dolastatin 15 binds in the vinca domain of tubulin as demonstrated by Hummel–Dreyer chromatography
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Báo cáo khoa học: Dolastatin 15 binds in the vinca domain of tubulin as demonstrated by Hummel–Dreyer chromatography
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