Inhibition of salt-induced actin polymerisation by thymosin β4 and its labelled derivatives assayed by falling ball viscometry
| Sample . | Time of fall (seconds) . |
|---|---|
| Buffer | 10±2 (n=5) |
| Actin | 155±9 (n=5) |
| Actin + thymosin β4 | 14±4 (n=5) |
| Actin + thymosin β4(OGC)2 | 12±3 (n=5) |
| Sample . | Time of fall (seconds) . |
|---|---|
| Buffer | 10±2 (n=5) |
| Actin | 155±9 (n=5) |
| Actin + thymosin β4 | 14±4 (n=5) |
| Actin + thymosin β4(OGC)2 | 12±3 (n=5) |
G-actin (4 μM) was incubated with equimolar amounts of the investigated peptides for 15 minutes at room temperature. Polymerisation was started by adding MgCl2 to a final concentration of 2 mM. Immediately after adding MgCl2 the mixture was filled into a glass capillary. After incubation for 4 hours at room temperature, viscosity was determined by falling ball viscometry.