Binding of maytansine to rat brain tubulin
作者： Frederika Mandelbaum-Shavit , Mary K. Wolpert-DeFilippes , David G. Johns
DOI: 10.1016/0006-291X(76)90958-X
关键词: Stereochemistry 、 Biophysics 、 Binding site 、 Vincristine 、 Colchicine 、 Tubulin 、 Chemistry 、 Rat brain 、 Cell biology 、 Biochemistry 、 Molecular biology
摘要: Abstract Maytansine and vincristine binding to crude rat brain tubulin is a temperature- ionic strength-dependent process. The K A values for of maytansine are 0.5 × 10 6 M −1 1.5 , respectively. competitively inhibits with i 0.4 −6 M. both drugs easily reversible. Unlabeled rapidly displaces the labeled drug whereas only about 75% bound was displaced by vincristine. Bound completely either or maytansine. Both appear share common site, although an additional site specific seems be present. Colchicine did not affect binding.
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