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. 1960 Nov;77(2):363–368. doi: 10.1042/bj0770363

The reduction of oxidized glutathione in erythrocyte haemolysates in pernicious anaemia

P C Jocelyn 1
PMCID: PMC1204993  PMID: 13790138

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Selected References

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

  1. ALVING A. S., CARSON P. E., FLANAGAN C. L., ICKES C. E. Enzymatic deficiency in primaquine-sensitive erythrocytes. Science. 1956 Sep 14;124(3220):484–485. doi: 10.1126/science.124.3220.484-a. [DOI] [PubMed] [Google Scholar]
  2. BEUTLER E. The hemolytic effect of primaquine and related compounds: a review. Blood. 1959 Feb;14(2):103–139. [PubMed] [Google Scholar]
  3. BHATTACHARYA S. K., ROBSON J. S., STEWART C. P. The determination of glutathione in blood and tissues. Biochem J. 1955 Aug;60(4):696–702. doi: 10.1042/bj0600696. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. COLLIER H. B., McRAE S. C. The amperometric determination of glutathione reductase activity in human erythrocytes. Can J Biochem Physiol. 1955 May;33(3):404–407. [PubMed] [Google Scholar]
  5. CONN E. E., VENNESLAND B. Glutathione reductase of wheat germ. J Biol Chem. 1951 Sep;192(1):17–28. [PubMed] [Google Scholar]
  6. FRANCOEUR M., DENSTEDT O. F. Metabolism of mammalian erythrocytes. VII. The glutathione reductase of the mammalian erythrocyte. Can J Biochem Physiol. 1954 Nov;32(6):663–669. [PubMed] [Google Scholar]
  7. GRUNERT R. R., PHILLIPS P. H. A modification of the nitroprusside method of analysis for glutathione. Arch Biochem. 1951 Feb;30(2):217–225. [PubMed] [Google Scholar]
  8. 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]
  9. JOCELYN P. C. The importance of thiol compounds in the causation of disease. Clin Chim Acta. 1958 Sep;3(5):401–418. doi: 10.1016/0009-8981(58)90031-7. [DOI] [PubMed] [Google Scholar]
  10. KASBEKAR D. K., LAVATE W. V., REGE D. V., SREENIVASAN A. A study of vitamin B12 protection in experimental thyrotoxicosis in the rat. Biochem J. 1959 Jul;72:374–383. doi: 10.1042/bj0720374. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. KASBEKAR D. K., SREENIVASAN A. Biosynthesis of glutathione by rat erythrocytes. Biochem J. 1959 Jul;72:389–395. doi: 10.1042/bj0720389. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. LING C. T., CHOW B. F. Effect of vitamin B12 on the levels of soluble sulfhydryl compounds in blood. J Biol Chem. 1953 May;202(1):445–456. [PubMed] [Google Scholar]
  13. LING C. T., CHOW B. F. The influence of vitamin B12 on carbohydrate and lipide metabolism. J Biol Chem. 1954 Feb;206(2):797–805. [PubMed] [Google Scholar]
  14. MARTIN H., McILWAIN H. Glutathione, oxidized and reduced, in the brain and in isolated cerebral tissue. Biochem J. 1959 Feb;71(2):275–280. doi: 10.1042/bj0710275. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. RALL T. W., LEHNINGER A. L. Glutathione reductase of animal tissues. J Biol Chem. 1952 Jan;194(1):119–130. [PubMed] [Google Scholar]
  16. REGISTER U. D. Effect of vitamin B12 on liver and blood non-protein sulfhydryl compounds. J Biol Chem. 1954 Feb;206(2):705–709. [PubMed] [Google Scholar]

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