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. 1960 Sep;76(3):556–562. doi: 10.1042/bj0760556

A protein disulphide reductase from pea seeds

M D Hatch 1, J F Turner 1
PMCID: PMC1204833  PMID: 13712218

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Selected References

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

  1. BARRON E. S. G., JOHNSON P. Studies on the mechanism of action of ionizing radiations. XI. Inactivation of yeast alcohol dehydrogenase by x-irradiation. Arch Biochem Biophys. 1954 Jan;48(1):149–153. doi: 10.1016/0003-9861(54)90316-1. [DOI] [PubMed] [Google Scholar]
  2. CONN E. E., VENNESLAND B. Glutathione reductase of wheat germ. J Biol Chem. 1951 Sep;192(1):17–28. [PubMed] [Google Scholar]
  3. FALCONE G., NICKERSON W. J. Identification of protein disulfide reductase as a cellular division enzyme in yeasts. Science. 1956 Oct 19;124(3225):722–723. doi: 10.1126/science.124.3225.722. [DOI] [PubMed] [Google Scholar]
  4. GERSCHMAN R., GILBERT D. L., NYE S. W., DWYER P., FENN W. O. Oxygen poisoning and x-irradiation: a mechanism in common. Science. 1954 May 7;119(3097):623–626. doi: 10.1126/science.119.3097.623. [DOI] [PubMed] [Google Scholar]
  5. GINTSBURG M. B., PANDRE E. M., BINUS N. M. Rol' sul'fgidril'nykh grupp i perekisnykh soedinenii v mekhanizme biologicheskogo deistviia ioniziruiushchego izlucheniia. Biokhimiia. 1957 May-Jun;22(3):467–475. [PubMed] [Google Scholar]
  6. HAGEMAN R. H., ARNON D. I. The isolation of triosephosphate dehydrogenase from pea seeds. Arch Biochem Biophys. 1955 Mar;55(1):162–168. doi: 10.1016/0003-9861(55)90554-3. [DOI] [PubMed] [Google Scholar]
  7. HATCH M. D., TURNER J. F. The aerobic inhibition of glycolysis in pea-seed extracts and its possible relationship to the Pasteur effect. Biochem J. 1959 Jul;72:524–532. doi: 10.1042/bj0720524. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. HATCH M. D., TURNER J. F. The mechanism of the reversible aerobic inhibition of glycolysis in a pea-seed extract. Biochem J. 1960 Apr;75:66–72. doi: 10.1042/bj0750066. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. HAUGAARD N., HESS M. E., ITSKOVITZ H. The toxic action of oxygen on glucose and pyruvate oxidation in heart homogenates. J Biol Chem. 1957 Aug;227(2):605–616. [PubMed] [Google Scholar]
  10. KAWAMURA N., DAN K. A cytochemical study of the sulfhydryl groups of sea urchin eggs during the first cleavage. J Biophys Biochem Cytol. 1958 Sep 25;4(5):615–619. doi: 10.1083/jcb.4.5.615. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. LADD J. N. The fermentation of lactic acid by a gram-negative coccus. Biochem J. 1959 Jan;71(1):16–22. doi: 10.1042/bj0710016. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. LANGDON R. G. Properties and mechanism of action of purified glutathione reductase. Biochim Biophys Acta. 1958 Nov;30(2):432–433. doi: 10.1016/0006-3002(58)90074-x. [DOI] [PubMed] [Google Scholar]
  13. MAPSON L. W., GODDARD D. R. The reduction of glutathione by plant tissues. Biochem J. 1951 Oct;49(5):592–601. doi: 10.1042/bj0490592. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. NICKERSON W. J., FALCONE G. Enzymatic reduction of disulfide bonds in cell wall protein of baker's yeast. Science. 1956 Aug 17;124(3216):318–319. doi: 10.1126/science.124.3216.318. [DOI] [PubMed] [Google Scholar]
  15. PIHL A., ELDJARN L., BREMER J. On the mode of action of x-ray protective agents. III. The enzymatic reduction of disulfides. J Biol Chem. 1957 Jul;227(1):339–345. [PubMed] [Google Scholar]
  16. RACKER E. Glutathione reductase from bakers' yeast and beef liver. J Biol Chem. 1955 Dec;217(2):855–865. [PubMed] [Google Scholar]
  17. RALL T. W., LEHNINGER A. L. Glutathione reductase of animal tissues. J Biol Chem. 1952 Jan;194(1):119–130. [PubMed] [Google Scholar]
  18. ROMANO A. H., NICKERSON W. J. Cystine reductase of pea seeds and yeasts. J Biol Chem. 1954 May;208(1):409–416. [PubMed] [Google Scholar]
  19. SAKAI H., DAN K. Studies on sulfhydryl groups during cell division of sea urchin egg. I. Glutatione. Exp Cell Res. 1959 Jan;16(1):24–41. doi: 10.1016/0014-4827(59)90192-2. [DOI] [PubMed] [Google Scholar]
  20. SANADI D. R., LANGLEY M., WHITE F. alpha-Ketoglutaric dehydrogenase. VII. The role of thioctic acid. J Biol Chem. 1959 Jan;234(1):183–187. [PubMed] [Google Scholar]
  21. TURNER J. F., MAPSON L. W. Aerobic inhibition of glycolysis. Nature. 1958 Jan 24;181(4604):270–270. doi: 10.1038/181270a0. [DOI] [PubMed] [Google Scholar]
  22. TURNER J. F. The biosynthesis of sucrose. Biochem J. 1957 Nov;67(3):450–456. doi: 10.1042/bj0670450. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. WEISSMAN N., SCHOENBACH E. B., ARMISTEAD E. B. The determination of sulfhydryl groups in serum. I. Methods and results on normal sera. J Biol Chem. 1950 Nov;187(1):153–165. [PubMed] [Google Scholar]

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