Abstract
A new 27/16 kDa form of cleaved actin was prepared by subtilisin cleavage between Ser234 and Ser235 of F(MgADP)-actin complexed with BeFx. The cleavage had little effect on actin-actin interactions as probed in polymerization measurements and by electron microscopy. In circular dichroism melting experiments the thermostability of F-actin was reduced by about 10°C by this cleavage. The in vitro motility and Vmax, but not Km, of actomyosin ATPase were decreased by about 20% upon 27/16 kDa cleavage of F-actin. The binding of tropomyosin to actin was unchanged by this modification.
Original language | English |
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Pages (from-to) | 149-151 |
Number of pages | 3 |
Journal | FEBS Letters |
Volume | 365 |
Issue number | 2-3 |
DOIs | |
State | Published - 29 May 1995 |
Keywords
- Actin
- Actomyosin interaction
- Proteolysis
- Structure-function relationship