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A novel kDa form of subtilisin cleaved actin: structural and functional consequences of cleavage between Ser 234 and Ser 235
Author(s) -
Vahdat Arash,
Miller Carl,
Phillips Martin,
Muhlrad Andras,
Reisler Emil
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00446-g
Subject(s) - cleavage (geology) , subtilisin , chemistry , actin , stereochemistry , microbiology and biotechnology , biology , biochemistry , enzyme , paleontology , fracture (geology)
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.