Abstract
Purified Artemia tubulin in the presence of neural microtubule-associated proteins and vinblastine, or with vinblastine alone, forms extensive coils. Reduction in temperature of a coil-containing solution to 4°C causes an increase in turbidity, which returns to previous levels once the solution is warmed. Examination of negatively stained samples indicates that the turbidity fluctuations are not accompanied by a pronounced change in coil structure nor by increased polymer formation. Bovine neural tubulin responds in the same way as Artemia tubulin to vinblastine and temperature. An interesting novel response to vinblastine, shared by tubulins from phylogenetically distinct organisms, is illustrated by our results.
Original language | English (US) |
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Pages (from-to) | 301-305 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 203 |
Issue number | 2 |
DOIs | |
State | Published - Jul 28 1986 |
Externally published | Yes |
Keywords
- (Artemia)
- Microtubule-associated protein
- Temperature effect
- Tubulin
- Vinblastine
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology