Abstract
A new 27/16 kDa form of cleaved actin was prepared by subtilisin cleavage between Ser 234 and Ser 235 of F(MgADP)-actin complexed with BeF x. 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 V max, but not K m, 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.
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