キハダマグロおよびコイのアクトミオシンからトリプシン消化によるHメロミオシンの調製の性質

概要

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Actomyosin (AM), when submitted to tryptic digestion, yielded fragments which remained bound to actin. The fragments were separated from actin by high concentration of ATP-Mg and collected in the supernatant by centrifugation When digestion of AM was conducted at 25°C for 10 min using trypsin in an amount of 1/200 (w/w) relative to AM, the enzymatically active fragments were isolated from yellowfin tuna AM. In the case of the enzymic activity of the fragments from carp AM was reduced even when the amount of trypsin was varied from 1/200 to 1/10, 000 (w/w) relative to AM. The fragments thus obtained were characterized by its enzymic activity, actin-binding properties, and chromatographic profile on Sephadex G-200. The proteolysis at 10°C instead of 25°C for 10 min using trypsin in an amount of 1/200 (w/w) relative to AM, was found to be favorable in priparing the enzymatically active fragments from carp AM. The fragments were further purified by salting with (NH4)2SO4 in the presence of 10mM ATP-Mg and then characterized by its enzymic activity, kinetic parameters (Vmax and Ka) of ATPase in actin activation, chromatographic profile on Sephadex G-200, and sedimentation constant It was thus shown that these fragments from yellowfin tuna and carp AMs were similar to heavy meromyosins from rabbit and skipjack tuna myosins, which have already been reported.
公益社団法人日本水産学会の論文