アクトミオシンの加熱乾燥によるβ構造への転位機構〔英文〕

概要

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The michanism of the transition of actomyosin (abbreviated as AM) to β-structure upon dehydration was studied. AM extracted from flatfish showed two rounded peaks at near 16° (2θ) and 29° in the X-ray diffraction pattern. Upon hot air dehydration at 60°C, the peak at 16° disappeared after 60min and two new peaks appeared at near 9° and at 28°; the former was rounded, while the latter was very sharp. After 120min, another rounded peak appeared at near 20°. In the presence of 3%, (w/w) glycerol, the round peak at 2° appeared after 60min and that at near 9°, after 180min, the two original peaks at near 16° and near 29° never being formed. Both IR-spectra of AM dehydrated in the presence and absence of glycerol for 180min showed amide I and II bands at near 1620cm-1 and near 1520cm-1, respectively. The results obtained in dolphin-fish resembled the spectral data described above very closely.
日本水産學會の論文