The influence of oxidation-reduction state on the kinetic stability of pig kidney general acyl-CoA dehydrogenase and other flavoproteins
| العنوان: | The influence of oxidation-reduction state on the kinetic stability of pig kidney general acyl-CoA dehydrogenase and other flavoproteins |
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| المؤلفون: | Colin Thorpe, M Madden, S M Lau |
| المصدر: | Biochemical Journal. 224:577-580 |
| بيانات النشر: | Portland Press Ltd., 1984. |
| سنة النشر: | 1984 |
| مصطلحات موضوعية: | Swine, Flavoprotein, Dehydrogenase, Flavin group, Kidney, Biochemistry, Electron-transferring flavoprotein, Acyl-CoA Dehydrogenase, Cofactor, Sodium dithionite, chemistry.chemical_compound, Acyl-CoA Dehydrogenases, Animals, heterocyclic compounds, Molecular Biology, Flavoproteins, biology, Dithionite, Acyl CoA dehydrogenase, Cell Biology, Kinetics, chemistry, biology.protein, Acyl Coenzyme A, Oxidation-Reduction, Research Article, Egg white |
| الوصف: | Pig kidney general acyl-CoA dehydrogenase is markedly stabilized against loss of flavin and activity in 7.3 M-urea or at 60 degrees C upon reduction with sodium dithionite or octanoyl-CoA. Electron transferring flavoprotein is similarly stabilized, whereas egg white riboflavin-binding protein loses flavin more readily on reduction. These and other data support the anticipated correlation between the kinetic stability of the holoproteins and the oxidation-reduction potential of their bound flavins. |
| تدمد: | 1470-8728 0264-6021 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cd9f527a1c48e8ab01b57302339d7276Test https://doi.org/10.1042/bj2240577Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....cd9f527a1c48e8ab01b57302339d7276 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 14708728 02646021 |
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