Wilson R R, Knowles F C
Arch Biochem Biophys. 1987 May 15;255(1):210-3. doi: 10.1016/0003-9861(87)90313-4.
Observation of rapid autoxidation of oxyhemoglobin (HbO2) from a deep-sea fish (Co-ryphaenoides acrolepis) prompted a survey of rates of autoxidation of HbO2 to methemoglobin in vitro from fishes inhabiting vastly different depths (1 to 3800 m) in order to discover any relationship between autoxidation rates and different environmental temperatures and pressures to which hemoglobins may be adapted. The rate of autoxidation was found to be sensitive to temperature in both deep- and shallow-living fishes. Hemoglobin appears to be thermally adapted since autoxidation was 10 times faster at all temperatures tested with HbO2 obtained from a cold-adapted fish (Coryphaenoides armatus variabilis) than from a comparatively warm-adapted one (Paralabrax nebulifer). High hydrostatic pressure does not affect autoxidation rates in either deep- or shallow-dwelling species. Rates of autoxidation may be intimately related to hemoglobin function thus providing a means for studying hemoglobin adaptation in poikilothermic vertebrates, especially among cold-adapted species.
对一种深海鱼类(长吻角鲾)的氧合血红蛋白(HbO₂)快速自动氧化的观察,促使人们对来自生活在截然不同深度(1至3800米)的鱼类的HbO₂在体外自动氧化为高铁血红蛋白的速率进行了调查,以便发现自动氧化速率与血红蛋白可能适应的不同环境温度和压力之间的任何关系。结果发现,无论是深海鱼类还是浅海鱼类,自动氧化速率对温度都很敏感。由于在用从适应寒冷的鱼类(变异长吻角鲾)获得的HbO₂进行的所有测试温度下,自动氧化速度比从相对适应温暖环境的鱼类(云斑副鲈)获得的HbO₂快10倍,因此血红蛋白似乎具有热适应性。高静水压力对深海或浅海物种的自动氧化速率均无影响。自动氧化速率可能与血红蛋白功能密切相关,从而为研究变温脊椎动物,特别是冷适应物种中的血红蛋白适应性提供了一种手段。