Carp myofibril was prepared from the ordinary muscle and stored in 0.1M KCl containing 5m
M NaN3 at 0°C.
The solubility of the myofibril in neutral 0.6M KCl decreased rapidly and reached a minimum level (about 20%) after storage for 3 weeks. EDTA
*2-ATPase activity of the myofibril decreased during the storage. Ca
2+ -and Mg
2+ -ATPase activities of the myofibril stored in an alkaline medium increased, but remained essentially unchanged at pH 6.1. Mg
2+ -ATPase activity assayed in the presence of EGTA
*2 increased during the storage over the pH range studied.
Ca
2+ -sensitivity of the myofibril stored in an alkaline medium was lost after storage for 2-3 weeks. The loss of Ca
2+ -sensitivity of the stored myofibril was not rostored by the addition of native tropomyosin. Electrophoretic patterns of native tropomyosin in the myofibril showed no change during the storage for up to 2-3 weeks. Active native tropomyosin could be obtained from the stored myofibril. Therefore, it seemed unlikely that the loss of Ca
2+ -sensitivity of the myofibril during ice-storage in the alkaline medium was due to the destruction or inactivation of native tropomyosin.
The changes in ATPase activities and in Ca
2+ -sensitivity of the myofibril blended in air and treated with oxidants or with NEM
*2 were similar to those of ice-stored myofibril. Furthermore, the changes in EDTA-and Mg
2+ -ATPase activities were reduced in the presence of 2-mer-captocthanol. These results suggested that the changes in ATPase activities and the loss of Ca
2+ -sensitivity of the myofibril during ice-storage, especially in alkaline medium may be due to the modification of actin-myosin interaction by the oxidation of the thiol groups of myosin moiety.
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