Tubulin in high-speed supernatants of brain undergoes an alternate form of polymerization into structures that resemble membranes rather than microtubules. The reaction required elevated temperature (37°C) and was prevented by 1mM CaCl2 or 10-4 M maytansine. The membraneous material was composed of tubulin (80%) and microtubule-associated proteins (8%) and contained phospholipids. The tubulin was identified on the basis of comigration in two-dimensional gel electrophoresis and colchicine-binding activity.
|Original language||English (US)|
|Number of pages||8|
|Journal||Biochemical and Biophysical Research Communications|
|Publication status||Published - May 14 1980|
ASJC Scopus subject areas
- Molecular Biology