Nichols J W, Weber L J
Oregon State University, Hatfield Marine Science Center, Newport 97365.
J Comp Physiol B. 1989;159(2):205-9. doi: 10.1007/BF00691741.
Myoglobins from rat, coho salmon (Oncorhynchus kisutch), buffalo sculpin (Enophrys bison) hearts, and yellowfin tuna (Thunnus albacares) red skeletal muscle were partially purified and their O2 binding affinities determined. Commercially prepared sperm whale myoglobin was employed as an internal standard. Tested at 20 degrees C, myoglobins from salmon and sculpin bound O2 with lower affinity than myoglobins from the rat or sperm whale. Oxygen binding studies at 12 degrees C and 37 degrees C suggest that this difference is adaptive, permitting myoglobins from cold-adapted fish to function at physiologically relevant temperatures. Taken together, purification and O2 binding data obtained in this study reveal a previously unrecognized diversity of myoglobin structure and function.
对大鼠、银大麻哈鱼（Oncorhynchus kisutch）、美洲杜父鱼（Enophrys bison）心脏以及黄鳍金枪鱼（Thunnus albacares）红色骨骼肌中的肌红蛋白进行了部分纯化，并测定了它们与氧气的结合亲和力。使用市售的抹香鲸肌红蛋白作为内标。在20摄氏度下进行测试时，鲑鱼和杜父鱼的肌红蛋白与氧气的结合亲和力低于大鼠或抹香鲸的肌红蛋白。在12摄氏度和37摄氏度下进行的氧气结合研究表明，这种差异具有适应性，使适应寒冷环境的鱼类的肌红蛋白能够在生理相关温度下发挥作用。综上所述，本研究获得的纯化和氧气结合数据揭示了此前未被认识到的肌红蛋白结构和功能的多样性。
