Evaluation of electron-transfer flavoprotein and α-lipoamide dehydrogenase redox states by two-channel fluorimetry and its application to the investigation of β-oxidation
作者： Wolfram S. Kunz
DOI: 10.1016/0005-2728(88)90134-X
关键词:
摘要: Abstract A new method permitting the simultaneous evaluation of redox states α-lipoamide dehydrogenase and electron-transfer flavoprotein in intact rat liver mitochondria by two-channel fluorimetry is described. It shown that correction for partial overlap emission spectra can readily be introduced after a calibration procedure performed. This was applied to investigation into regulation palmitoylcarnitine oxidation. found presence rotenone, malonate buffer mitochondrial NAD-system, β-oxidation flux sensitive variations state respiratory chain electron carriers at low NAD reduction. Therefore, concept control caused solely no longer sustained.
elsevier.com
sci-hub.se 参考文章(26)
Reinhart Heinrich, Tom A. Rapoport, A Linear Steady-State Treatment of Enzymatic Chains Critique of the Crossover Theorem and a General Procedure to Identify Interaction Sites with an Effector FEBS Journal. ,vol. 42, pp. 97- 105 ,(1974) , 10.1111/J.1432-1033.1974.TB03319.X
J D Beckmann, F E Frerman, The effects of pH, ionic strength, and chemical modifications on the reaction of electron transfer flavoprotein with an acyl coenzyme A dehydrogenase. Journal of Biological Chemistry. ,vol. 258, pp. 7563- 7569 ,(1983) , 10.1016/S0021-9258(18)32215-4
S.V. Pande, On Rate-controlling Factors of Long Chain Fatty Acid Oxidation Journal of Biological Chemistry. ,vol. 246, pp. 5384- 5390 ,(1971) , 10.1016/S0021-9258(18)61919-2
R Scholz, R G Thurman, J R Williamson, B Chance, T Bücher, Flavin and pyridine nucleotide oxidation-reduction changes in perfused rat liver. I. Anoxia and subcellular localization of fluorescent flavoproteins. Journal of Biological Chemistry. ,vol. 244, pp. 2317- 2324 ,(1969) , 10.1016/S0021-9258(19)78228-3
W G Gustafson, B A Feinberg, J T McFarland, Energetics of beta-oxidation. Reduction potentials of general fatty acyl-CoA dehydrogenase, electron transfer flavoprotein, and fatty acyl-CoA substrates. Journal of Biological Chemistry. ,vol. 261, pp. 7733- 7741 ,(1986) , 10.1016/S0021-9258(19)57462-2
F Di Virgilio, G F Azzone, Activation of site I redox-driven H+ pump by exogenous quinones in intact mitochondria. Journal of Biological Chemistry. ,vol. 257, pp. 4106- 4113 ,(1982) , 10.1016/S0021-9258(18)34692-1
L Lumeng, J Bremer, E J Davis, Suppression of the mitochondrial oxidation of (-)-palmitylcarnitine by the malate-aspartate and alpha-glycerophosphate shuttles. Journal of Biological Chemistry. ,vol. 251, pp. 277- 284 ,(1976) , 10.1016/S0021-9258(17)33875-9
Kazuko MAEDA-YORITA, Kenji AKI, Effect of Nicotinamide Adenine Dinucleotide on the Oxidation-Reduction Potentials of Lipoamide Dehydrogenase from Pig Heart Journal of Biochemistry. ,vol. 96, pp. 683- 690 ,(1984) , 10.1093/OXFORDJOURNALS.JBCHEM.A134886
H Osmundsen, J Bremer, A spectrophotometric procedure for rapid and sensitive measurements of β-oxidation. Demonstration of factors that can be rate-limiting for β-oxidation Biochemical Journal. ,vol. 164, pp. 621- 633 ,(1977) , 10.1042/BJ1640621
M Husain, M T Stankovich, B G Fox, Measurement of the oxidation-reduction potentials for one-electron and two-electron reduction of electron-transfer flavoprotein from pig liver Biochemical Journal. ,vol. 219, pp. 1043- 1047 ,(1984) , 10.1042/BJ2191043