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Biochemical Studies on Changes in Fish Muscle Proteins Following Temperature Acclimation

温度适应后鱼肌肉蛋白变化的生化研究

基本信息

批准号：
02454081
负责人：
WATABE Shugo
金额：
$ 4.29万
依托单位：
The University of Tokyo
依托单位国家：
日本
项目类别：
Grant-in-Aid for General Scientific Research (B)
财政年份：
1990
资助国家：
日本
起止时间：
1990 至 1991
项目状态：
已结题

项目摘要

Since fish myofibrillar proteins account for over 50% in total muscle proteins, the feasibility of various kinds of fish meat for food processing and their stability during storage are regarded to be greatly influenced by the properties of myofibrillar proteins. This study was performed to answer the questions on which components and parts are most critical in changes of myofibrillar proteins of carp and goldfish during temperature acclimation, thus providing fisheries industry with valuable and foundamental information on fish muscles as food materials.1. Several individuals of carp were acclimated to either 10 or 30ﾟC for a minimum of 1 month and subjected to the preparation of myofibrils. Myofibrillar Mg^<2+>-ATPase activity of 10ﾟC-acclimated carp was significantly higher than that of 30ﾟC-acclimated fish when assayed at the same reaction temperatures. In contrast, the thermal stability at 40ﾟC of myofibrillar Ca^<2+->-ATPase of 10ﾟC-acclimated carp was several times lower than tha … More t of 30ﾟC-acclimated one. The similar results were obtained when acclimated goldfish were subjected to the same experiments.2. Myosin and its subfragment-1 (Sl) from 10ﾟC-acclimated carp showed a higher maximal initial velocity (Vmax) in actin-activated Mg^<2+>-ATPase activity than the 30ﾟC-acclimated counterparts, respectively, in a good agreement with the differences observed in myfibrillar Mg^<2+>-ATPase activity between the two acclimated groups. The 30ﾟC-acclimated myosin and Sl were again more thermostable than the 10ﾟC-acclimated counterparts, respectively.3. When a filamentous part of the myosin molecule, rod, was subjected to a limited proteolysis using alpha-chymotrypsin, the 10ﾟC-acclimated carp exhibited one L-meromyosin band in SDS-PAGE analysis. On the other hand, the 30ﾟC-acclimated carp gave three L-meromyosin bands. one of which was identical to the 10ﾟC-acclimated L-meromyosin.4. Peptide maps of myosin and Sl heavy chains and rod performed in SDS-gels were clearly different between 10ﾟC-and 30ﾟC-acclimated carp, suggesting that the primary structure of carp myosin molecule is altered during temperature acclimation. Less

由于鱼肉肌原纤维蛋白占肌肉总蛋白的50%以上，因此，肌原纤维蛋白的性质被认为对各种鱼肉的食品加工可行性及其在储存过程中的稳定性有很大影响。本研究的目的是为了回答鲤鱼和金鱼在温度驯化过程中肌原纤维蛋白质变化的关键组分和部位，从而为鱼类肌肉作为饲料提供有价值的基础信息.几个人的鲤鱼适应10或30摄氏度至少1个月，并进行肌原纤维的准备。在相同的反应温度下，10 ℃驯化鲤鱼的肌原纤维Mg^<2+>-ATPase活性显著高于30 ℃驯化鱼。相反，10 ℃驯化鲤鱼肌原纤维Ca^<2+->-ATP酶在40 ℃的热稳定性比对照低几倍。 ...更多信息 30 ℃的t-驯化1。对驯化金鱼进行同样的实验，也得到了类似的结果. 10 ° C驯化鲤鱼的肌球蛋白及其亚片段-1（Sl）肌动蛋白激活的Mg^<2+>-ATP酶活性的最大初始速度（Vmax）分别高于30 ° C驯化的鲤鱼，这与两个驯化组之间观察到的肌原纤维Mg^<2+>-ATP酶活性的差异非常一致。30 ℃驯化的肌球蛋白和S1再次比10 ℃驯化的对应物更耐热。当肌球蛋白分子的丝状部分，杆，进行有限的蛋白质水解使用α-糜蛋白酶，10 μ C-驯化鲤鱼表现出一个L-裂肌球蛋白带在SDS-PAGE分析。另一方面，30 ℃驯化的鲤鱼给出了三条L-肌球蛋白带。其中一个与10 μ C-驯化的L-裂肌球蛋白相同。10 ℃和30 ℃驯化鲤鱼的肌球蛋白和S1重链和杆状蛋白的SDS-凝胶肽图明显不同，表明鲤鱼肌球蛋白分子的一级结构在温度驯化过程中发生了变化。少