ホタテガイ閉殻筋横紋部から調製したミオシンの性質

• 資料種別: 記事
• タイトル: ホタテガイ閉殻筋横紋部から調製したミオシンの性質
• 著者・編者: 西田 清義
• 著者標目: 西田 清義
• 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）: 43(3) 1977.03
• 掲載巻: 43
• 掲載号: 3
• 掲載ページ: p335～341
• 掲載年月日（W3CDTF）: 1977-03
• 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: 生物学--生理・生化学・生物物理--核酸・蛋白質・酵素 ; 農林水産学--水産--水産生物
• 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）: 1817469; http://id.ndl.go.jp/bib/1817469
• 整理区分コード: 632

• 要約等: Myosin was prepared from the striated adductor muscle of giant ezo scallop, <i>patinopecten yessoensis</i>, by the original method of BÁRÁNY <i>et al</i>.<br> This myosin showed the typical biological activity of myosin as already known tor rabbit myosin; that is, high ATP hydrolyzing activity and actin-binding ability.<br> The actin-bingding ability of this myosin was examined by measuring the increase in ATP-sensitivity, superprecipitation, the enhancement of Mg²⁺-ATPase and the stabilization of Ca²⁺-ATPase for thermal denaturation.<br> The first order rate constants for the thermal denaturation of Ca²⁺-ATPase (K_D) were determined to be 22×10^-4•sec^-1 at 30°C, and 61-128×10^-4•sec^-1 at 35°C, while those of rabbit myosin were 1.5×10^-4•sec^-1 at 30°C, and 3.7×10^-4•sec^-1 at 35°C.<br> SDS-gel electrophoresis indicated that a small amount of paramyosin and a trace of actin remained in this myosin preparation.
• DOI: 10.2331/suisan.43.335
• 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: Myosin was prepared from the striated adductor muscle of giant ezo scallop, <i>patinopecten yessoensis</i>, by the original method of BÁRÁNY <i>et al</i>.<br> This myosin showed the typical biological activity of myosin as already known tor rabbit myosin; that is, high ATP hydrolyzing activity and actin-binding ability.<br> The actin-bingding ability of this myosin was examined by measuring the increase in ATP-sensitivity, superprecipitation, the enhancement of Mg²⁺-ATPase and the stabilization of Ca²⁺-ATPase for thermal denaturation.<br> The first order rate constants for the thermal denaturation of Ca²⁺-ATPase (K_D) were determined to be 22×10^-4•sec^-1 at 30°C, and 61-128×10^-4•sec^-1 at 35°C, while those of rabbit myosin were 1.5×10^-4•sec^-1 at 30°C, and 3.7×10^-4•sec^-1 at 35°C.<br> SDS-gel electrophoresis indicated that a small amount of paramyosin and a trace of actin remained in this myosin preparation.
• DOI: 10.2331/suisan.43.335; https://doi.org/10.2331/suisan.43.335
• 関連情報（URI）: https://agriknowledge.affrc.go.jp/RN/2010144695; http://id.ndl.go.jp/bib/1817469; https://ndlsearch.ndl.go.jp/books/R000000004-I1817469
• 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）: 1817469; http://id.ndl.go.jp/bib/1817469
• NII論文ID: 130000920231