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
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- Material Type
- 記事
- Author/Editor
- 大泉 徹山村 寛仁新井 健一
- Periodical title
- 日本水産学会誌 / 日本水産学会 編
- No. or year of volume/issue
- 48(2) 1982.02
- Volume
- 48
- Issue
- 2
- Pages
- p219～226
- Publication date of volume/issue (W3CDTF)
- 1982-02
- ISSN (Periodical Title)
- 0021-5392
- ISSN-L (Periodical Title)
- 0021-5392
- Publication (Periodical Title)
- 東京 : 日本水産学会
- Place of Publication (Country Code)
- JP
- Text Language Code
- jpn
- NDLC
- Target Audience
- 一般
- Article Type
- 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
- Holding library
- 国立国会図書館
- Call No.
- Z18-345
- Data Provider (Database)
- 国立国会図書館 : 国立国会図書館雑誌記事索引
- Bibliographic ID (NDL)
- 2440407
- Bibliographic Record Category (NDL)
- 632
- Summary, etc.
- 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
- Access Restrictions
- インターネット公開
- Data Provider (Database)
- 科学技術振興機構 : J-STAGE
- Summary, etc.
- 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
- Related Material (URI)
- Is Referenced By
- Effect of Cryoprotectants and a Reducing Reagent on the Stability of Actomyosin during Ice Storage
- Data Provider (Database)
- 国立情報学研究所 : CiNii Research
- Original Data Provider (Database)
- 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
- Bibliographic ID (NDL)
- 2440407
- NAID
- 13000154706210021720309