Binding of the microtubule protein, tubulin, to hydrophobic groups immobilized on octyl sepharose has been investigated. The results indicate that tubulin binds to octyl sepharose in a time-, teperature-, and concentration-dependent manner. Binding is multiphasic, with one fast phase and at least two slow phases, and is influenced by the presence of antimitotic drugs. Colchicine, vinblastine and podophyllotoxin enhance the fast binding of tubulin with very little effect on the slow binding. Pre-incubation of tubulin with the apolar probe, bis(1,8-anilinonaphthalene-sulfonate) (BisANS) enhances both the rapid and slow phases of binding of tubulin to octyl sepharose. 1,8-Anilinonaphthalenesulfonate, the monomer of BisANS, has no effect. These results are consistent with a model for tubulin decay which involves the appearance of hydrophobic sites with time.
|Original language||English (US)|
|Number of pages||7|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Jun 15 1987|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology