@article{oai:nagasaki-u.repo.nii.ac.jp:00017683,
 author = {橘, 勝康 and 鈴木, 秀一 and 八木, 基明 and 三嶋, 敏雄 and 原, 研治 and 槌本, 六良},
 issue = {4},
 journal = {日本水産学会誌, Bulletin of the Japanese Society of Scientific Fisheries},
 month = {},
 note = {養殖マダイ普通筋α-アクチニン抗体を作成し, これを用いて養殖マダイ氷蔵中における普通筋中α-アクチニンの分解をSDS-PAGEとイムノブロッティングで解析した。作成したα-アクチニン抗体はマダイ普通筋中のα-アクチニンのみならず, そのパパイン分解物とも反応性を示した。本抗体は免疫電顕による観察で, 筋原線維のZ線に特異的に反応し, 他の細胞内小器官等には反応を認めなかった。普通筋中α-アクチニンは氷蔵1日目から自己消化され, 5日目以降ではすべて分子量90kDa∿100kDaの成分に限定分解されていた。, Anti-α-actinin IgG was prepared from rat serum immunized with purified α-actinin in the ordinary muscle of red sea bream. Anti-α-actinin IgG showed immune reactivity against not only α-actinin in ordinary muscle but also papain-digests of the α-actinin. According to immunoelectron microscopic method, α-actinin was detected on Z line of ordinary muscle cells and non-specific reactions were not detected on another organelles. The changes of α-actinin in the ordinary muscle of cultured red sea bream during storage in ice were examined by SDS-PAGE followed by its immunoblotting. It was found that the limited digestion of α-actinin in ordinary muscle of cultured red sea bream started on day one in ice, then, native α-actinin was not detected on day 5 and 7. These results suggested that the weakening of Z-disks in ordinary muscle was caused by the disappearance of α-actinin and resulted in the softness of the flesh texture of cultured red sea bream., 日本水産学会誌 = Bulletin of the Japanese Society of Scientific Fisheries. 2001, 67(4), p.723-727},
 pages = {723--727},
 title = {養殖マダイの氷蔵中における普通筋中 α-アクチニンの限定分解},
 volume = {67},
 year = {2001}
}