The influence of oxidation-reduction state on the kinetic stability of pig kidney general acyl-CoA dehydrogenase and other flavoproteins
Keyword(s):
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.
1966 ◽
Vol 241
(18)
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pp. 4180-4185
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1981 ◽
Vol 256
(15)
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pp. 7756-7763
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Keyword(s):
2021 ◽
Vol 18
(11)
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pp. 5977
1952 ◽
Vol 8
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pp. 114
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1940 ◽
Vol 23
(8)
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pp. 725-744
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1943 ◽
Vol 26
(6)
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pp. 515-523
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2002 ◽
Vol 90
(3)
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pp. 273-281
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