Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1969 Feb;111(3):309–315. doi: 10.1042/bj1110309

Studies in the enzymology of glutathione metabolism in human erythrocytes

R C Jackson 1
PMCID: PMC1187513  PMID: 4388010

Abstract

Spectrophotometric assay methods are described for glutathione synthetase, γ-glutamylcysteine synthetase and γ-glutamyl transpeptidase of erythrocytes. The contents of these enzymes in normal human erythrocytes are reported. Erythrocyte glutathione synthetase is inhibited by ADP; this inhibition is competitive with respect to ATP. γ-Glutamylcysteine synthetase is subject to feedback inhibition by GSH, and is also inhibited by NADH, and to a lesser extent by NAD+ and NADPH. This enzyme is irreversibly inactivated by cysteamine.

Full text

PDF
309

Selected References

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

  1. Ball C. R. Estimation and identification of thiols in rat spleen after cysteine or glutathione treatment: relevance to protection against nitrogen mustards. Biochem Pharmacol. 1966 Jul;15(7):809–816. doi: 10.1016/0006-2952(66)90157-2. [DOI] [PubMed] [Google Scholar]
  2. Boivin P., Galand C. La synthèse du glutathion au cours de l'anémie hémolytique congénitale avec déficit en glutathion réduit. Déficit congénital en glutathion-synthérase érythrocytaire? Nouv Rev Fr Hematol. 1965 Sep-Oct;5(5):707–720. [PubMed] [Google Scholar]
  3. CLIFFE E. E., WALEY S. G. Acidic peptides of the lens. 6. Metabolism of gamma-glutamyl peptides in subcellular fractions of rabbit liver. Biochem J. 1961 Apr;79:118–128. doi: 10.1042/bj0790118. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. DIMANT E., LANDSBERG E., LONDON I. M. The metabolic behavior of reduced glutathione in human and avian erythrocytes. J Biol Chem. 1955 Apr;213(2):769–776. [PubMed] [Google Scholar]
  5. ELDJARN L., BREMER J., BORRESEN H. C. The reduction of disulphides by human erythrocytes. Biochem J. 1962 Jan;82:192–197. doi: 10.1042/bj0820192. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Ehrhart H., Scheffel G. Untersuchungen über den Leukocytenstoffwechsel. 3. NAD-(Nicotinamid-adenin-dinucleotid)-Gehalt isolierter Leukocyten und Krankheitsverlauf menschlicher chronischer Leukämien unter cytostatischer Therapie mit C 73. Klin Wochenschr. 1966 Mar 15;44(6):307–314. doi: 10.1007/BF01752278. [DOI] [PubMed] [Google Scholar]
  7. HARRAP K. R., SPEED D. E. SOME BIOCHEMICAL ASPECTS OF LEUKAEMIAS: THE APPEARANCE OF A SOLUBLE DISULPHIDE IN THE BLOOD IN CHRONIC GRANULOCYTIC LEUKAEMIA. Br J Cancer. 1964 Dec;18:809–817. doi: 10.1038/bjc.1964.94. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Jacob H. S., Jandl J. H. Effects of sulfhydryl inhibition on red blood cells. 3. Glutathione in the regulation of the hexose monophosphate pathway. J Biol Chem. 1966 Sep 25;241(18):4243–4250. [PubMed] [Google Scholar]
  9. 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]
  10. MANDELES S., BLOCK K. Enzymatic synthesis of gamma-glutamylcysteine. J Biol Chem. 1955 Jun;214(2):639–646. [PubMed] [Google Scholar]
  11. MILLS G. C. Hemoglobin catabolism. I. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative breakdown. J Biol Chem. 1957 Nov;229(1):189–197. [PubMed] [Google Scholar]
  12. PATTERSON J. W., LAZAROW A. Determination of glutathione. Methods Biochem Anal. 1955;2:259–278. doi: 10.1002/9780470110188.ch9. [DOI] [PubMed] [Google Scholar]
  13. Révész L., Modig H. Cysteamine-induced increase of cellular glutathione-level: a new hypothesis of the radioprotective mechanism. Nature. 1965 Jul 24;207(995):430–431. doi: 10.1038/207430a0. [DOI] [PubMed] [Google Scholar]
  14. SILBER R., GABRIO B. W., HUENNEKENS F. M. Studies on normal and leukemic leukocytes. III. Pyridine nucleotides. J Clin Invest. 1962 Feb;41:230–234. doi: 10.1172/JCI104474. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES