Fischer J C, Ruitenbeek W, Berden J A, Trijbels J M, Veerkamp J H, Stadhouders A M, Sengers R C, Janssen A J
Clin Chim Acta. 1985 Nov 29;153(1):23-36. doi: 10.1016/0009-8981(85)90135-4.
Procedures are described for the estimation of the succinate:ubiquinone oxidoreductase and succinate:phenazine methosulfate oxidoreductase activities in post-nuclear supernatants of human skeletal muscle homogenates using 2,6-dichlorophenol indophenol as the terminal electron acceptor. The influence of ionic strength and of sucrose upon these assays and upon the succinate:cytochrome c oxidoreductase activity has been investigated. Sucrose markedly interferes with the activation of the succinate dehydrogenase complex. Succinate:cytochrome c oxidoreductase activity and succinate:phenazine methosulfate oxidoreductase activity are inhibited by increasing concentrations of ions and of sucrose. Our results lead us to propose the existence of a single acceptor site for phenazine methosulfate at the succinate dehydrogenase complex, not involved in the physiological electron flux across ubiquinone. Estimation of the enzymatic activities mentioned above allows differential investigation of the functional integrity of a large part of the respiratory chain in patients suspected of suffering from a neuromuscular disorder.
本文描述了使用2,6-二氯酚靛酚作为末端电子受体，对人骨骼肌匀浆核后上清液中琥珀酸：泛醌氧化还原酶和琥珀酸：吩嗪硫酸甲酯氧化还原酶活性进行测定的方法。研究了离子强度和蔗糖对这些测定以及对琥珀酸：细胞色素c氧化还原酶活性的影响。蔗糖显著干扰琥珀酸脱氢酶复合物的激活。随着离子和蔗糖浓度的增加，琥珀酸：细胞色素c氧化还原酶活性和琥珀酸：吩嗪硫酸甲酯氧化还原酶活性受到抑制。我们的结果使我们提出，在琥珀酸脱氢酶复合物处存在一个单一的吩嗪硫酸甲酯受体位点，它不参与跨泛醌的生理电子传递。对上述酶活性的测定有助于对疑似患有神经肌肉疾病的患者呼吸链大部分功能完整性进行差异研究。
