Kinetics of mitochondrial flavoprotein and pyridine nucleotide in perfused heart.

Kinetics of mitochondrial flavoprotein and pyridine nucleotide in perfused heart.
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灌注心脏中线粒体黄素蛋白和吡啶核苷酸的动力学。

DOI:
10.1152/ajplegacy.1972.223.6.1497-s
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发表时间:
1972
期刊:
The American journal of physiology
影响因子:
--
通讯作者:
K. Johnson
K. Johnson
中科院分区:
--
文献类型:
--
作者:
Britton;Chance;Irving;A.;Salkovitz;Aristid;G.;B.;K. Johnson

文献摘要

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欧文·钱斯Salkovitz和Aristid G. B。- VACH。灌流心脏线粒体贾沃蛋白和吡啶核苷酸的动力学。Am. J.Physiol.213(l):207-218. 1972.-线粒体电子传递的快速激活可以识别其代谢能量负荷的性质和大小。闪光光解激活CO抑制的细胞色素氧化酶在氧的存在下启动氧化还原吡啶核苷酸(PN)和黄素蛋白(Fp)和响应率高,在高ADP和Ca 2f水平。PN和Fp的光解响应的分数程度指示在光解闪光时氧已经扩散到的含有细胞色素a& 0的总线粒体群体的分数。对于PN和Fp响应,该分数为4X.5,并且被认为是组织中氧扩散有效性的有用指标。如此快速的反应(<O. 1组)在体外ADP + Pi存在下未观察到,需要线粒体外Ca 2+浓度。本文综述了快速扰动完整组织生理和生化状态的技术,并介绍了线粒体细胞色素as-CO化合物在氧气存在下的闪光光解方法,以及线粒体PN和Fp的氧化还原状态的记录。
CHANCE, BWTON, IRVING A. SALKOVITZ, AND ARISTID G. B. ~VACH. Kinetics of mitochondrial javoprotein and pyridine nucleotide in perfused heart. Am. J. Physiol. 213(l): 207-218. 1972.-Fast activation of mitochondrial electron transport can identify the nature and magnitude of their metabolic energy load. Flash photolysis activation of CO-inhibited cytochrome oxidase in the presence of oxygen initiates oxidation of reduced pyridine nucleotide (PN) and flavoprotein (Fp) and the rate of the response is high at high ADP and Ca 2f levels. The fractional extent of the photolysis response of PN and Fp indicates the fraction of the total mitochondrial population containing cytochrome a&O to which oxygen has diffused at the time of the photolysis flash. This fraction is 4X.5 for PN and Fp responses and is considered to be a useful indicator of the effectiveness of oxygen diffusion in the tissue. Such a rapid response ( <O. 1 set) is not observed in vitro in the presence of ADP + Pi, extramitochondrial Ca2+ concentrations are required. Techniques for the rapid perturbation of the physiological and biochemical states of intact tissues are reviewed and the method of flash photolysis of the mitochondrial cytochrome as-CO compound in the presence of oxygen is described, together with the recording of the oxidation-reduction states of mitochondn’al PN and Fp.