Premium
Absence of 7‐acetyl taxol binding to unassembled brain tubulin
Author(s) -
Takoudju Martin,
Wright Michel,
Chenu Jacques,
Guéritte-Voegelein Françoise,
Guénard Daniel
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80875-5
Subject(s) - tubulin , chemistry , microbiology and biotechnology , biochemistry , microtubule , biology
The effect of taxol on microtubule proteins at 0°C is controversial. In order to determine if taxol is unable to bind to unassembled tubulin, as has been hypothesized, the binding of [ 3 H]acetyl taxol has been studied using equilibrium microdialysis. Ac‐taxol bound to microtubules at 37°C and the binding remained stable when the temperature was lowered to 0°C. Ac‐taxol bound also at 0°C to microtubules stabilized with rhazinilam. In contrast, there was no binding of Ac‐taxol to unassembled tubulin, either free tubulin at 0°C or tubulin, complexed with several microtubule poisons, at 0 and 37°C.