Changes in ATPase Activities and Other Properties of Carp Myofibrillar Proteins during Ice-Storage

SEKI Nobuo, NARITA Norihiro

doi:10.2331/suisan.46.207

Carp muscle was minced or chopped into small blocks and stored in ice for up to 16 days. Triton-washed myofibrils were prepared from the at-desath and stored muscles.<br> EDTA-ATPase activity of the myofibrils from the minced muscles decreased rapidly, while Ca²⁺- and Mg²⁺-ATPase activities decreased gradually during ice-storage with the exception that Mg²⁺-ATPase activity in the presence of EGTA increased. The increase in this ATPase activity was accompanied with a loss of Ca²⁺-sensitivity of the myofibrils. Little changes, however, occurred in ATPase activities of the myofibrils from the muscle blocks during ice-storage. SDS-polyacrylamide gel electrophoresis showed that the myofibrils from the fresh and stored muscles were similar in composition.<br> The change in Ca²⁺-ATPase activity of myosin B obtained from the stored muscles by extraction from the myofibrils paralleled that of the myofibrils during the storage. Mg²⁺-ATPase activity of the myofibrils from the fresh muscles was higher than that of the myosin B, but this difference reduced with increasing storage period of the muscles. Myosin B. obtained from the stored muscles contained aggregates more than the fresh myosin B. Myosin B aggregates sedimented by centrifugation at 20, 000×g for 20min had higher Mg²⁺-ATPase activity and lower EDTA-ATPase activity and lower Ca²⁺-sensitivity than myosin B in supernatant. The viscosity, ATP-sensitivity, and sedimentation behaviour of the myosin B were also measured.

Changes in ATPase Activities and Other Properties of Carp Myofibrillar Proteins during Ice-Storage

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