水産動物肉に関する研究-29-

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In order to investigate the necessary conditions for the extensive extraction of pure myosin from fish muscles, the composition of myosins in the muscle extracts obtained under various conditions was determined by salting-out analysis. The composition of myosins extractable with 0.6M NaCl from a homogenate of horsemackerel muscle varied widely with the pH of the extractant solution. When the homogenate was extracted at slightly acidic pH, two large peaks were observed on the salting-out curves; the one precipitated between 28 and 38% saturations of ammonium sulphate was assumed to be actomyosin and the other precipitated between 35 and 48% saturations was assumed to be myosin. At the neutral pH, the actomyosin peak became more predominant, while the other peak corresponding to myosin became less apparent. When the extraction was carried out at an alkaline pH of 9.2, these two peaks were still apparent, but a new large peak presumed to be actin appeared between 10 and 20% saturations of ammonium sulphate. The rise and fall of the myosin and actomyosin peaks appearing in the slightly acidic extracts were also affected by the extent of the mechanical destruction of muscle tissue; the more coarsely the muscle was minced, the less amount of actomyosin component was observed in the 0.6M NaCl extracts. When the file-fish muscle allowed to pass through a chopper-plate of the mesh larger than 3 mm, we obtained myosins free from actomyosin. However, this result may be insufficient for justifying the applicability to fishes of the HASSELBACH's fractionation procedure for rabbit, since from such a coarsely minced muscle only a part of myosin is separated by a single extraction and since repeating extraction unavoidably contaminates the extracts with actomyosin. HASSELBACH'S observation that the splitting-action of pyrophosphate on actomyosin particles contributes to the separation of myosin from coarsely minced rabbit muscle failed to apply the fish muscles studied in this work. This seems to suggest that the stroma of fish muscle is much smaller in amount than that of rabbit muscle and can not keep the actin from going into solution, and that the splitting-action of pyrophosphate is not so marked as usually accepted and the majority of actomyosin does not dissociate into two components, myosin and actin.
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水産動物肉に関する研究-29-

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