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. 1957 Nov;67(3):406–416. doi: 10.1042/bj0670406

Essential role of thiol groups in aldehyde dehydrogenases

A O M Stoppani 1, C Milstein 1
PMCID: PMC1200171  PMID: 13479397

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Selected References

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

  1. ALBERT A. Quantitative studies of the avidity of naturally occurring substances for trace metals. II. Amino-acids having three ionizing groups. Biochem J. 1952 Mar;50(5):690–697. doi: 10.1042/bj0500690. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. BARRON E. S. G., LEVINE S. Oxidation of alcohols by yeast alcohol dehydrogenase and by the living cell; the thiol groups of the enzyme. Arch Biochem Biophys. 1952 Nov;41(1):175–187. doi: 10.1016/0003-9861(52)90518-3. [DOI] [PubMed] [Google Scholar]
  3. BONNER W. D. Activation of the succinic dehydrogenase-cytochrome system. Biochem J. 1954 Feb;56(2):274–285. doi: 10.1042/bj0560274. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. GURD F. R., WILCOX P. E. Complex formation between metallic cations and proteins, peptides and amino acids. Adv Protein Chem. 1956;11:311–427. doi: 10.1016/s0065-3233(08)60424-6. [DOI] [PubMed] [Google Scholar]
  5. Hopkins F. G., Morgan E. J., Lutwak-Mann C. The influence of thiol groups in the activity of dehydrogenases. II: With an addendum on the location of dehydrogenases in muscle. Biochem J. 1938 Oct;32(10):1829–1848. doi: 10.1042/bj0321829. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. KACHMAR J. F., BOYER P. D. Kinetic analysis of enzyme reactions. II. The potassium activation and calcium inhibition of pyruvic phosphoferase. J Biol Chem. 1953 Feb;200(2):669–682. [PubMed] [Google Scholar]
  7. KAPLAN N. O., CIOTTI M. M. Direct evidence for a diphosphopyridine nucleotide-hydroxylamine complex with horse liver alcohol dehydrogenase. J Biol Chem. 1954 Nov;211(1):431–445. [PubMed] [Google Scholar]
  8. KOEPPE O. J., BOYER P. D., STULBERG M. P. On the occurrence, equilibria, and site of acyl-enzyme formation of glyceraldehyde-3-phosphate dehydrogenase. J Biol Chem. 1956 Apr;219(2):569–583. [PubMed] [Google Scholar]
  9. SEEGMILLER J. E. Triphosphopyridine nucleotide-linked aldehyde dehydrogenase from yeast. J Biol Chem. 1953 Apr;201(2):629–637. [PubMed] [Google Scholar]
  10. SEGAL H. L., BOYER P. D. The role of sulfhydryl groups in the activity of D-glyceraldehyde 3-phosphate dehydrogenase. J Biol Chem. 1953 Sep;204(1):265–281. [PubMed] [Google Scholar]
  11. STADTMAN E. R., NOVELLI G. D., LIPMANN F. Coenzyme A function in and acetyl transfer by the phosphotransacetylase system. J Biol Chem. 1951 Jul;191(1):365–376. [PubMed] [Google Scholar]
  12. STOPPANI A. O., ACTIS A. S., DEFERRARI J. O., GONZALEZ E. L. The role of sulphydryl groups of yeast carboxylase. Biochem J. 1953 Jun;54(3):378–390. doi: 10.1042/bj0540378. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. STOPPANI A. O., MILSTEIN C. Specific protection of the thiol groups of aldehyde dehydrogenases by pyridine-nucleotide coenzymes. Biochim Biophys Acta. 1957 Jun;24(3):655–657. doi: 10.1016/0006-3002(57)90270-6. [DOI] [PubMed] [Google Scholar]
  14. TERAYAMA H., VESTLING C. S. Sodium sulfide inhibition of liver lactic dehydrogenase. Biochim Biophys Acta. 1956 Jun;20(3):586–587. doi: 10.1016/0006-3002(56)90371-7. [DOI] [PubMed] [Google Scholar]
  15. VAN EYS J., KAPLAN N. O. Yeasl alcohol dehydrogenase. I. The effect of pyridine derivatives on the reaction. Biochim Biophys Acta. 1957 Mar;23(3):574–581. doi: 10.1016/0006-3002(57)90379-7. [DOI] [PubMed] [Google Scholar]

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