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. 1951 Apr;48(4):458–467. doi: 10.1042/bj0480458

The stabilization of d-amino-acid oxidase by flavin-adenine dinucleotide, substrates and competitive inhibitors

K Burton 1
PMCID: PMC1275351  PMID: 14838867

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Selected References

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

  1. Delory G. E., King E. J. The rate of enzymic hydrolysis of phosphoric esters: 2. Relation of structure to dissociation constant, Michaelis constant, and rate of hydrolysis. Biochem J. 1943;37(5):547–550. doi: 10.1042/bj0370547. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Keilin D., Hartree E. F. Properties of azide-catalase. Biochem J. 1945;39(2):148–157. doi: 10.1042/bj0390148. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Needham D. M. The adenosinetriphosphatase activity of myosin preparations. Biochem J. 1942 Feb;36(1-2):113–120. doi: 10.1042/bj0360113. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Proceedings of the Biochemical Society. Biochem J. 1948;42(1):i.1–i.x. [PMC free article] [PubMed] [Google Scholar]
  5. WEBER G. Fluorescence of riboflavin and flavin-adenine dinucleotide. Biochem J. 1950 Jun-Jul;47(1):114–121. doi: 10.1042/bj0470114. [DOI] [PMC free article] [PubMed] [Google Scholar]

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