魚の死後経過に伴なうミオシン区たん白の変性-IV : ミオシン区たん白の組成と活性

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Succeeding to the previous papers1), post-mortem change of fish myofibrillar proteins was studied by means of ultracentrifugal sedimentation of 0.6 M KCl extracts and superprecipitation of actomyosin preparation in the presence of ATP. The fishes examined were the sea-bass, flatfish, yellowtail and skipjack. They were killed by cutting their spinal cords to obtain the ordinary muscle. A portion of the muscle was immediately extracted as the prerigor sample. The other portions were kept at 0-2°C for the proper periods from several hours to a few days as the rigor or postrigor samples. Ultracentrifugal sedimentation at ca. 50, 000 r.p.m. suggests that the dominant component in the 0.6 M KCl extracts is actomyosin at the postrigor phase regardless of fish species, but either actomyosin or myosin at the prerigor and rigor phases (Figs. 2-4). The patterns at 40, 000 r.p.m. show the so-called gel-fraction at the rigor and postrigor phases, which is not seen at the prerigor phase (Fig. 4). Superprecipitation of actomyosin gel is found on all samples irrespective of post-mortem stage (Figs. 6-7). In the earlier paper1, 3), it was pointed out that fish are distinguished into two types by the post-mortem changes in intrinsic viscosity and flow birefringence of the myosins fraction. The difference between these two types of fish, however, was not distinct, so far as ultra-centrifugal sedimentation pattern of the 0.6 M KCl extracts or superprecipitation of actomyosin gel concerns.
公益社団法人日本水産学会の論文

魚の死後経過に伴なうミオシン区たん白の変性-IV : ミオシン区たん白の組成と活性

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