魚類ミオシンおよびミオシンBのATPase活性に及ぼすN-エチルマレイミド修飾の影響

• 資料種別: 記事
• タイトル: 魚類ミオシンおよびミオシンBのATPase活性に及ぼすN-エチルマレイミド修飾の影響
• 著者・編者: 渡辺 孝博; 関 伸夫
• 著者標目: 渡辺 孝博; 関 伸夫
• タイトル（掲載誌）: 日本水産学会誌 / 日本水産学会 編
• 巻号年月日等（掲載誌）: 48(1) 1982.01
• 掲載巻: 48
• 掲載号: 1
• 掲載ページ: p57～63
• 掲載年月日（W3CDTF）: 1982-01
• ISSN（掲載誌）: 0021-5392
• ISSN-L（掲載誌）: 0021-5392
• 出版事項（掲載誌）: 東京 : 日本水産学会
• 出版地（国名コード）: JP
• 本文の言語コード: jpn
• NDLC: ZR26
• 対象利用者: 一般
• 記事種別、記事分類: 記事分類: 食品工学--水産食品 ; 生物学--生理・生化学・生物物理--核酸・蛋白質・酵素 ; 医学--生化学
• 所蔵機関: 国立国会図書館
• 請求記号: Z18-345
• 連携機関・データベース: 国立国会図書館 : 国立国会図書館雑誌記事索引; https://ndlsearch.ndl.go.jp
• 書誌ID（NDLBibID）: 2437293; http://id.ndl.go.jp/bib/2437293
• 整理区分コード: 632

• 要約等: The Ca²⁺ -ATPase activity of fish myosin was activated by N-ethylmaleimide (NEM) treatment, while the EDTA-ATPase activity was inhibited. These changes indicate that fish myosin, like rabbit myosin, contains first reactive thiol groups (SH₁).<br> On the other hand, myosin SH₁ in myosin B system was completely unreactive with NEM under the conditions where the association of actin-myosin occurred, i.e., at physiological ionic strength and pH, and in the absence of ATP. These results suggest that myosin SH₁ in fish muscle may be masked with actin under the conditions of postmortem storage. The Mg²⁺ -ATPase activtity of myosin B, however, increased by NEM treatment under the conditions where SH₁ was unreactive. <br> It was also found that the thermal stability of the ATPase activity of fish myosin B. on storage at high ionic strength, was decreased remarkably by the NEM treatment. This thermal instability of the NEM treated myosin B may be due to the dissociation of myosin and actin.
• DOI: 10.2331/suisan.48.57
• オンライン閲覧公開範囲: インターネット公開
• 連携機関・データベース: 科学技術振興機構 : J-STAGE; http://www.jstage.jst.go.jp

• 要約等: The Ca²⁺ -ATPase activity of fish myosin was activated by N-ethylmaleimide (NEM) treatment, while the EDTA-ATPase activity was inhibited. These changes indicate that fish myosin, like rabbit myosin, contains first reactive thiol groups (SH₁).<br> On the other hand, myosin SH₁ in myosin B system was completely unreactive with NEM under the conditions where the association of actin-myosin occurred, i.e., at physiological ionic strength and pH, and in the absence of ATP. These results suggest that myosin SH₁ in fish muscle may be masked with actin under the conditions of postmortem storage. The Mg²⁺ -ATPase activtity of myosin B, however, increased by NEM treatment under the conditions where SH₁ was unreactive. <br> It was also found that the thermal stability of the ATPase activity of fish myosin B. on storage at high ionic strength, was decreased remarkably by the NEM treatment. This thermal instability of the NEM treated myosin B may be due to the dissociation of myosin and actin.
• DOI: 10.2331/suisan.48.57; https://doi.org/10.2331/suisan.48.57
• 関連情報（URI）: https://agriknowledge.affrc.go.jp/RN/2030242594; http://id.ndl.go.jp/bib/2437293; https://ndlsearch.ndl.go.jp/books/R000000004-I2437293
• 連携機関・データベース: 国立情報学研究所 : CiNii Research; https://cir.nii.ac.jp/
• 提供元機関・データベース: Japan Link Center; https://japanlinkcenter.org/top; 学術機関リポジトリデータベース; https://irdb.nii.ac.jp; 雑誌記事索引データベース; https://ndlsearch.ndl.go.jp; Crossref; https://www.crossref.org; CiNii Articles
• 書誌ID（NDLBibID）: 2437293; http://id.ndl.go.jp/bib/2437293
• NII論文ID: 130001547143