Although myoglobin (Mb) has been considered to be one of the well-characterized proteins, screening of post-genomic era databases revealed the lack of adequate information on teleost Mbs. The present study was aimed to investigate stability and functional features of Mbs from three teleosts of the same family. To unfold how primary structure influences the stability and function of proteins, Mbs were purified from the dark muscles of three carangids, namely, yellowtail, greater amberjack, and silver trevally. Thermostabilities measured by circular dichroism (CD) spectrometry revealed species-specific thermal denaturation pattern, i.e., silver trevally > yellowtail > greater amberjack Mbs. On the other hand, autoxidation rate constants of the ferrous forms of those three carangid Mbs showed positive correlation between the ferrous state of the heme iron and rising temperature. The order of autoxidation rate was in the order of greater amberjack > yellowtail > silver trevally Mbs. The finding of the present study denotes that the thermal stability is not necessarily correlated with the functional stability of carangid Mbs even though their primary structures shared high homology (84–94%).

尽管肌红蛋白（Mb）被认为是特征鲜明的蛋白质之一，但对基因组后时代数据库的筛选显示，关于硬骨鱼Mbs缺乏足够的信息。本研究旨在调查来自同一家族的三个硬骨鱼的Mb的稳定性和功能特征。为了揭示一级结构如何影响蛋白质的稳定性和功能，从三种尾鳍的黑肌肉中纯化了多溴联苯，它们分别是黄尾鱼，greater鱼和tr银。通过圆二色性（CD）光谱测量的热稳定性显示了物种特定的热变性模式，即银tr>黄尾>更大的M Mbs。另一方面，这三种类胡萝卜素Mb的亚铁形式的自氧化速率常数显示，血红素铁的亚铁态与温度升高呈正相关。自氧化速率的顺序为琥珀鱼>黄尾鱼>银三叶草Mbs。本研究的发现表明，即使类胡萝卜素的主要结构具有很高的同源性（84-94％），热稳定性也不一定与它们的功能稳定性相关。