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Literature DB >> 6517865

The influence of oxidation-reduction state on the kinetic stability of pig kidney general acyl-CoA dehydrogenase and other flavoproteins.

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.

Entities: Chemical Species

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Year: 1984 PMID： 6517865 PMCID： PMC1144467 DOI： 10.1042/bj2240577

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

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References

18 in total

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Authors: T P SINGER; E B KEARNEY
Journal: Arch Biochem Date: 1950-11

2. Differential reactivity of the two active site cysteine residues generated on reduction of pig heart lipoamide dehydrogenase.

Authors: C Thorpe; C H Williams
Journal: J Biol Chem Date: 1976-06-25 Impact factor: 5.157

3. The nature of the biochemical lesion in avian renal riboflavinuria. 3. The isolation and characterization of the riboflavin-binding protein from egg albumen.

Authors: H M Farrell; M F Mallette; E G Buss; C O Clagett
Journal: Biochim Biophys Acta Date: 1969-12-23

10. Measurement of the oxidation-reduction potentials for one-electron and two-electron reduction of electron-transfer flavoprotein from pig liver.

Authors: M Husain; M T Stankovich; B G Fox
Journal: Biochem J Date: 1984-05-01 Impact factor: 3.857

The influence of oxidation-reduction state on the kinetic stability of pig kidney general acyl-CoA dehydrogenase and other flavoproteins.

1. The L-amino acid oxidases of snake venom. II. Isolation and characterization of homogeneous L-amino acid oxidase.

2. Differential reactivity of the two active site cysteine residues generated on reduction of pig heart lipoamide dehydrogenase.

3. The nature of the biochemical lesion in avian renal riboflavinuria. 3. The isolation and characterization of the riboflavin-binding protein from egg albumen.

4. A potentiometric study of the flavin semiquinone equilibrium.

5. The binding of flavin derivatives to the riboflavin-binding protein of egg white. A kinetic and thermodynamic study.

6. A method for resolution of general acyl-coenzyme A dehydrogenase apoprotein.

7. Purification and properties of electron-transferring flavoprotein from pig kidney.

8. Dissociation and assembly of pyridine nucleotide transhydrogenase from Azotobacter vinelandii.

9. Interaction of long-chain acyl-CoA analogs with pig kidney general acyl-CoA dehydrogenase.

10. Measurement of the oxidation-reduction potentials for one-electron and two-electron reduction of electron-transfer flavoprotein from pig liver.