常氧和缺氧条件下工作大鼠心脏呼吸酶氧化还原状态及肌红蛋白氧合作用的监测
Monitoring of redox-state of respiratory enzymes and myoglobin oxygenation in the working rat heart in normoxia and oxygen deficiency.
作者信息
Zündorf J, Tauschek D, Frank K, Ito K, Nioka S, Kessler M, Chance B
机构信息
Institut für Physiologie und Kardiologie, Universität Erlangen-Nürnberg.
出版信息
Adv Exp Med Biol. 1992;317:583-92. doi: 10.1007/978-1-4615-3428-0_69.
The cellular oxygen supply in the isolated, hemoglobin-free perfused, working rat heart can be determined by measurements of myoglobin oxygenation. However, for a precise analysis of mitochondrial hypoxia and anoxia (pO2 < 0.01 Torr) redox-state of respiratory enzymes must be known. By use of the EMPHO (Frank et al. 1989) it is possible to perform a high speed spectrometry within very small tissue volumes. Because of the characteristic absorption spectra of oxygenated and deoxygenated myoglobin and of the oxidized and reduced cytochrome aa3 within the wavelength interval from 500 to 630 nm it is possible to isolate these two pigments from the remission spectra and to determine the oxygenation state of myoglobin and the redox-state of cytochrom aa3.
在分离的、无血红蛋白灌注的工作大鼠心脏中，细胞氧供应可通过测量肌红蛋白氧合来确定。然而，要精确分析线粒体缺氧和无氧状态（pO2 < 0.01托），必须了解呼吸酶的氧化还原状态。通过使用EMPHO（弗兰克等人，1989年），可以在非常小的组织体积内进行高速光谱分析。由于在500至630纳米波长范围内，氧合和脱氧肌红蛋白以及氧化和还原细胞色素aa3具有特征吸收光谱，因此可以从反射光谱中分离出这两种色素，并确定肌红蛋白的氧合状态和细胞色素aa3的氧化还原状态。
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