氧化还原状态对猪肾通用酰基辅酶A脱氢酶及其他黄素蛋白动力学稳定性的影响
The influence of oxidation-reduction state on the kinetic stability of pig kidney general acyl-CoA dehydrogenase and other flavoproteins.
作者信息
Madden M, Lau S M, Thorpe C
出版信息
Biochem J. 1984 Dec 1;224(2):577-80. doi: 10.1042/bj2240577.
Abstract
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.
摘要
猪肾总酰基辅酶A脱氢酶在用连二亚硫酸钠或辛酰辅酶A还原后，在7.3M尿素中或60℃时，针对黄素和活性丧失具有显著的稳定性。电子传递黄素蛋白同样稳定，而蛋清黄素结合蛋白在还原时更容易失去黄素。这些以及其他数据支持了全蛋白的动力学稳定性与其结合黄素的氧化还原电位之间预期的相关性。
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