Abstract
The differences between myosin B extracted from fresh muscle with Weber-Edsall solution and myosin B type protein from the muscle stored at 4°C post-mortem were investigated by the measurement of ATPase activity, ATP-sensitivity, salting-out curves, chromatographic patterns on triethylaminoethyl (TEAE)-cellulose, viscosity and ultra-centrifugation diagrams. As compared with myosin B from fresh muscle and myosin B type protein from post-rigor muscle, myosin B type protein from rigor muscle showed relatively high values of ATPase activity, ATP-sensitivity and reduced viscosity, and moreover, was remarkably different in salting-out curves, precipitating gradually from ammonium sulfate of lower concentration than that in others. The differences between myosin B from fresh muscle and myosin B type protein from post-rigor muscle were clearly demonstrated by chromatography and sedimentation data.
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