SUMMARY Changes in selected physicochemical properties of the myosin B fraction of turkey muscle were followed during a 44‐hr post‐rigor aging period. Sedimentation patterns of myosin B fractions prepared 48 hr after death indicated a decrease in a high‐molecular‐weight component thought to he myosin B gel. It is concluded that myosin B fractions lose gel‐forming ability with resolution of rigor. Density‐gradient centrifugal patterns showed small increases in slowly sedimenting components of myosin B fractions with aging. These components were. high in ATP‐ase activity in the presence of calcium ions and showed no reduction of viscosity with addition of ATP. Some evidence favors the concept of dissociation of myosin B into myosin A and actin with resolution of rigor. This dissociation, however, may also represent disruption of myosin R gel formed during and after extraction from muscle.
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Scharpf et al. (1966) studied this question.
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