Abstract
It was previously reported that the turbid protein extracts from fish muscle contained a gel fraction. In order to investigate the relationship between the gel fraction and myofibrillar protein, some properties of the former were examined. The gel fraction was prepared from frozen- or ice-stored muscles of both the flatfish, Kareius bicoloratus, and Alaska pollack, Theragra charcogramma, by extraction using KCl-phosphate buffer (I=0.5, pH 7.2) and cen-trifugal sedimentation at 30, 000-40, 000×g. The absorption curve of the gel fraction was similar to that of actomyosin. The gel fraction did not show streaming birefringence by OKADA's apparatus. On addition of ATP to the gel fraction at low ionic strength, superprecipitation occurred forming a loose slurry-like precipitate. The viscosity of the redispersed solution (I=0.5) of the gel fraction fell sharply on addition of ATP, but the ATP sensitivity values were not very high. The gel fraction had Mg-ATPase activity at low ionic strength (0.03 M KCl). These properties of the gel fraction are similar to that of actomyosin with the exception of streaming birefringence. As a result, the author considers that the gel fraction may contain an aggregated protein which involves myofibrillar protein and that the shape of the aggregate may not be so thread-like.
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