サバ筋原繊維の加熱変性に対するアミノ酸類および糖類の協同保護効果
デジタルデータあり（科学技術振興機構）
すぐに読む
J-STAGE
全国の図書館の所蔵
国立国会図書館以外の全国の図書館の所蔵状況を表示します。
所蔵のある図書館から取寄せることが可能かなど、資料の利用方法は、ご自身が利用されるお近くの図書館へご相談ください
その他
J-STAGE
デジタルCiNii Research
検索サービスデジタル連携先のサイトで、CiNii Researchが連携している機関・データベースの所蔵状況を確認できます。
書誌情報
この資料の詳細や典拠（同じ主題の資料を指すキーワード、著者名）等を確認できます。
- 資料種別
- 記事
- 著者・編者
- 大泉 徹山村 寛仁新井 健一
- 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(2) 1982.02
- 掲載巻
- 48
- 掲載号
- 2
- 掲載ページ
- p219～226
- 掲載年月日（W3CDTF）
- 1982-02
- 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
- 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 ; 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
- 書誌ID（NDLBibID）
- 2440407
- 整理区分コード
- 632
- 要約等
- The protective effect of amino acid and joint protective effects of various mixtures, which included sorbitol, sucrose, Na-Glu, Na-Asp, or Gly, on the thermal stability of chub mackerel myofibrils have been studied. The first order rate constant (<i>k<sub>D</sub></i>) for inactivation of myofibrillar Ca-ATPase was determined in each case.<br> Plotting the logarithm of <i>k<sub>D</sub></i> against the concentration (M) of amino acid, a single linear relation was obtained for Gly, Ala, and β-Ala, whereas a linear relation with two steps was found for Na-Glu and Na-Asp. The slope (<i>E</i>) of the graph of log <i>k<sub>D</sub></i> versus molarity of amino acid revealed that the protective effect against the denaturation of myofibrils becomes lowerin the order of: Na-Glu (0-0.75M), Na-Asp (0-0.75M), Gly=Ala=β-Ala (0-1.5M), Na-Glu (0.75-2.5M), Na-Asp (0.75-2.5M), Pro (0-1.25M), Gln=Asn (0-0.2M). Arginine. histidine and glycylglycine were ineffective.<br> The decreases in log <i>k<sub>D</sub></i>, showed that the protective effects against the denaturation of myofibrils were nearly addivtive for all pair combination selected from among Na-Glu, Na-Asp, Gly, sorbitol and surose.<br> The effect of amino acid and the cooperating effect of the studied mixtures were practically unchanged over the temperature range (25-45°C) at which the myofibrils were treated.
- DOI
- 10.2331/suisan.48.219
- 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
- 要約等
- The protective effect of amino acid and joint protective effects of various mixtures, which included sorbitol, sucrose, Na-Glu, Na-Asp, or Gly, on the thermal stability of chub mackerel myofibrils have been studied. The first order rate constant (<i>k<sub>D</sub></i>) for inactivation of myofibrillar Ca-ATPase was determined in each case.<br> Plotting the logarithm of <i>k<sub>D</sub></i> against the concentration (M) of amino acid, a single linear relation was obtained for Gly, Ala, and β-Ala, whereas a linear relation with two steps was found for Na-Glu and Na-Asp. The slope (<i>E</i>) of the graph of log <i>k<sub>D</sub></i> versus molarity of amino acid revealed that the protective effect against the denaturation of myofibrils becomes lowerin the order of: Na-Glu (0-0.75M), Na-Asp (0-0.75M), Gly=Ala=β-Ala (0-1.5M), Na-Glu (0.75-2.5M), Na-Asp (0.75-2.5M), Pro (0-1.25M), Gln=Asn (0-0.2M). Arginine. histidine and glycylglycine were ineffective.<br> The decreases in log <i>k<sub>D</sub></i>, showed that the protective effects against the denaturation of myofibrils were nearly addivtive for all pair combination selected from among Na-Glu, Na-Asp, Gly, sorbitol and surose.<br> The effect of amino acid and the cooperating effect of the studied mixtures were practically unchanged over the temperature range (25-45°C) at which the myofibrils were treated.
- DOI
- 10.2331/suisan.48.219
- 関連情報（URI）
- 参照
- Effect of Cryoprotectants and a Reducing Reagent on the Stability of Actomyosin during Ice Storage
- 連携機関・データベース
- 国立情報学研究所 : CiNii Research
- 提供元機関・データベース
- Japan Link Center学術機関リポジトリデータベース雑誌記事索引データベースCrossrefCiNii ArticlesCiNii ArticlesCrossref
- 書誌ID（NDLBibID）
- 2440407
- NII論文ID
- 13000154706210021720309