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A chimera (domain I of SCa M-4 and domains II-IV of SCa M-1) behaved like SCa M4, and analysis of site-specific mutants of SCa M-1 indicated that K30E and G40D mutations were responsible for the reduction in activation of MLCK.

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Myosin (19) and MLCK (20) were purified from chicken gizzard smooth muscle.

Polyclonal anti-Ca M antibody was purchased from Santa Cruz Biotechnology and used at 0 dilution.

Activated MLCK phosphorylates the 20-k Da light chains of myosin II at Ser, triggering cross-bridge cycling and the development of force (11, 12).

The availability of the different plant Ca M isoforms provides very useful tools for studying the mechanism of activation of MLCK and other Ca M target enzymes.

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