Huang Ming-Chih, Lee Cheng-Linn, Ochiai Yoshihiro, Watabe Shugo
Department of Biological Sciences and Technology, National University of Tainan, 33, Sec.2, Shu-Lin St., Tainan, Taiwan, 700-05, Republic of China.
Department of Aquatic Bioscience, Graduate School of Agricultural and Life Sciences, University of Tokyo, Tokyo, Bunkyo, 113-8657, Japan.
Fish Physiol Biochem. 2019 Jun;45(3):1189-1202. doi: 10.1007/s10695-019-00632-7. Epub 2019 Apr 3.
In order to investigate the species-specific heat tolerance of tropical fishes, the thermodynamic properties of muscle tropomyosin, a member of myofibrillar proteins, were compared among milkfish, tilapia, grouper, and mudskipper. The purified tropomyosins were subjected to differential scanning calorimetry and circular dichroism spectrometry. To unveil the relationship between the stability and the amino acid sequences, the muscle tropomyosin genes of the four species were also cloned, and their deduced amino acid sequences were compared. Thermodynamic analysis revealed that the milkfish tropomyosin showed lower refolding ability after thermal denaturation, compared with those of the other species. The amino acid sequences of these tropomyosins were similar to each other, with the identity being in the range of 95-96%.
为了研究热带鱼类的种特异性耐热性，对肌原纤维蛋白成员之一的肌肉原肌球蛋白的热力学性质，在遮目鱼、罗非鱼、石斑鱼和弹涂鱼之间进行了比较。对纯化的原肌球蛋白进行差示扫描量热法和圆二色光谱分析。为了揭示稳定性与氨基酸序列之间的关系，还克隆了这四个物种的肌肉原肌球蛋白基因，并比较了它们推导的氨基酸序列。热力学分析表明，与其他物种相比，遮目鱼原肌球蛋白在热变性后表现出较低的重折叠能力。这些原肌球蛋白的氨基酸序列彼此相似，同一性在95%-96%范围内。
