Abstract
The assembly of whole microtubule protein, derived from bovine brain extracts by multiple cycles of temperature-induced assembly and disassembly, exhibits a lag phase in which there is a characteristic, transient drop in the turbidity. This drop is inconsistent with the direct participation of ring-like structures in microtubule assembly, and warming microtubule protein in the presence of GDP unmasks the kinetics of this dissociation phenomenon. These and other data suggest that rings are enthalpy-stabilized and are unlikely intermediates in the entropy-driven self-assembly of microtubules.
Original language | English (US) |
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Pages (from-to) | 1885-1889 |
Number of pages | 5 |
Journal | Topics in Catalysis |
Volume | 95 |
Issue number | 4 |
DOIs | |
State | Published - Jan 1 1980 |
Externally published | Yes |
ASJC Scopus subject areas
- Catalysis
- Chemistry(all)
- Biochemistry
- Biophysics
- Molecular Biology