Studies on the proteins of fish skeletal muscle. 5. Molecular weight and shape of cod fibrillar proteins

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Abstract
Solutions of unaggregated cod myosin were prepared by ultracentrifugal separation after dissociation of cod actomyosin with adenosine triphosphate or pyrophosphate. The sedimentation and diffusion coefficients of cod myosin at infinite dilution were measured and the molecular weight and shape calculated from these data with the measured partial specific volume. Investigation of the diffusion behavior both in stationary boundaries and in boundaries in the ultracentrifuge indicate that the preparations of cod myosin are heterogeneous. The molecular weight of cod myosin was also determined by the Archibald procedure and the axial ratio assessed from the intrinsic viscosity. Some aspects of the aggregation of cod myosin were examined. Cod actin was purified in the ultracentrifuge and its sedimentation coefficient determined. The order of magnitude of the molecular weight of cod actomyosin was determined from turbidity measurements. The size and shape of the cod fibrillar proteins are very similar to those of the rabbit proteins. The unusual properties of the fish proteins cannot be explained therefore on this basis.