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. 1957 Sep;67(1):146–155. doi: 10.1042/bj0670146

Preparation and properties of highly purified diaphorase

Nerina Savage 1
PMCID: PMC1200122  PMID: 13471525

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. AKESON A., THEORELL H. Molecular weight and FMN content of crystallin old yellow enzyme. Arch Biochem Biophys. 1956 Nov;65(1):439–448. doi: 10.1016/0003-9861(56)90204-1. [DOI] [PubMed] [Google Scholar]
  2. BEINERT H. New evidence for the occurrence of free radicals in flavoprotein catalysis. Biochim Biophys Acta. 1956 Jun;20(3):588–590. doi: 10.1016/0006-3002(56)90372-9. [DOI] [PubMed] [Google Scholar]
  3. BURTON K. The stabilization of D-amino acid oxidase by flavin-adenine dinucleotide, substrates and competitive inhibitors. Biochem J. 1951 Apr;48(4):458–467. doi: 10.1042/bj0480458. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Corran H. S., Green D. E., Straub F. B. On the catalytic function of heart flavoprotein. Biochem J. 1939 May;33(5):793–801. doi: 10.1042/bj0330793. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. DOLIN M. I. Evidence for an enzyme-substrate complex between pyridine nucleotides and DPNH peroxidase flavoprotein. Arch Biochem Biophys. 1956 Feb;60(2):499–508. doi: 10.1016/0003-9861(56)90456-8. [DOI] [PubMed] [Google Scholar]
  6. Dewan J. G., Green D. E. Coenzyme factor-a new oxidation catalyst. Biochem J. 1938 Mar;32(3):626–639. doi: 10.1042/bj0320626. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. EDELHOCH H., HAYAISHI O., TEPLY L. J. The preparation and properties of a soluble diphosphopyridine nucleotide cytochrome c reductase. J Biol Chem. 1952 May;197(1):97–104. [PubMed] [Google Scholar]
  8. Green D. E., Dewan J. G., Leloir L. F. The beta-hydroxybutyric dehydrogenase of animal tissues. Biochem J. 1937 Jun;31(6):934–949. doi: 10.1042/bj0310934. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Green D. E., Dewan J. G. The reversible oxidation and reduction of coenzyme I. Biochem J. 1937 Jul;31(7):1069–1073. doi: 10.1042/bj0311069. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Green D. E., Needham D. M., Dewan J. G. Dismutations and oxidoreductions. Biochem J. 1937 Dec;31(12):2327–2352. doi: 10.1042/bj0312327. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. KEILIN D., HARTREE E. F. Specificity of glucose oxidase (notatin). Biochem J. 1952 Jan;50(3):331–341. doi: 10.1042/bj0500331. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Keilin D., Hartree E. F. Properties of glucose oxidase (notatin): Addendum. Sedimentation and diffusion of glucose oxidase (notatin). Biochem J. 1948;42(2):221–229. [PMC free article] [PubMed] [Google Scholar]
  13. Lockhart E. E. Diaphorase (coenzyme factor). Biochem J. 1939 Apr;33(4):613–617. doi: 10.1042/bj0330613. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. MAHLER H. R., SARKAR N. K., VERNON L. P. Studies on diphosphopyridine nucleotide-cytochrome c reductase. II. Purification and properties. J Biol Chem. 1952 Dec;199(2):585–597. [PubMed] [Google Scholar]
  15. SINGER T. P., KEARNEY E. B. The L-amino acid oxidases of snake venom; prosthetic group of the L-amino acid oxidase of moccasin venom. Arch Biochem. 1950 Jul;27(2):348–363. [PubMed] [Google Scholar]
  16. SLATER E. C. The components of the dihydrocozymase oxidase system. Biochem J. 1950 Apr;46(4):484–499. doi: 10.1042/bj0460484. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. STRITTMATTER P., VELICK S. F. The isolation and properties of microsomal cytochrome. J Biol Chem. 1956 Jul;221(1):253–264. [PubMed] [Google Scholar]
  18. Straub F. B. Isolation and properties of a flavoprotein from heart muscle tissue. Biochem J. 1939 May;33(5):787–792. doi: 10.1042/bj0330787. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. VELICK S. F., STRITTMATTER P. The oxidation-reduction stoichiometry and potential of microsomal cytochrome. J Biol Chem. 1956 Jul;221(1):265–275. [PubMed] [Google Scholar]
  20. WHITBY L. G. A new method for preparing flavin-adenine dinucleotide. Biochem J. 1953 Jun;54(3):437–442. doi: 10.1042/bj0540437. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. WHITBY L. G. Enzymic formation of a new riboflavin derivative. Nature. 1950 Sep 16;166(4220):479–480. doi: 10.1038/166479b0. [DOI] [PubMed] [Google Scholar]

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