Ca2+-induced binding of calpain-2 to myofibrils: Preliminary results in pork longissimus thoracis muscle supporting a role on myofibrillar protein degradation

The aim of this study was to investigate the role Ca2+ in process calpain-2 becoming associated myofibrils and potential myofibril-bound calpain degrade myofibrillar proteins. Different concentrations were applied mixed with partially purified calpain-2. induced binding a concentration-dependent manner. half-maximal requirements for proteolysis 0.60 mM 0.29 mM, respectively. To proteolytic activity calpain, mixture briefly incubated Ca2+. Unbound removed by washing Ca2+-free buffer. maintained degraded desmin when re-activated In conclusion, results suggest that an increase will activate induce myofibrils. Subsequently, is relatively tightly bound proteolytically active.