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Glutathionuria: γ-Glutamyl transpeptidase deficiency

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A mentally retarded young woman with severe behaviour problems was found to excrete large amounts of glutathione due to a generalized γ-glutamyl transpeptidase deficiency. As in the only other case described in detail, plasma levels and renal reabsorption of the amino acids were normal. In the parents' urine, plasma and leukocytes, enzyme activity was normal but in their cultured fibroblasts it was below the minimum for the control range. An autosomal recessive mode of inheritance is suggested. The implications of these findings for the possible role of the γ-glutamyl cycle in amino acid transport are briefly discussed.

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  1. Beutler, E. Glutathione deficiency, pyroglutamic acidemia and amino acid transport.N. Engl. J. Med. 295 (1976) 441

  2. Carson, N. A. J., Dent, C. E., Field, C. M. B. and Gaull, G. E. Homocystinuria. Clinical and pathological review of ten cases.J. Pediatr. 66 (1965) 565

  3. Donovan, B. T. The behavioural actions of the hypothalamic peptides: a review.Psychol. Med. 8 (1978) 305

  4. Ersser, R. S. and Krywawych, S. Simple and rapid high resolution thin-layer electrophoresis of amino acids.Med. Lab. Technol. 31 (1974) 325

  5. Goodman, S. I., Mace, J. W. and Pollak, S. Serum gamma-glutamyl transpeptidase deficiency.Lancet 1 (1971) 234

  6. Levy, H. L. Genetic screening.Adv. Hum. Genet. 4 (1973) 1

  7. Lowry, O. H., Rosebrough, N. J., Farr, A. L. and Randall, R. J. Protein measurement with the Folin-phenol reagent.J. Biol. Chem. 193 (1951) 265

  8. Meister, A. On the enzymology of amino acid transport.Science 180 (1973) 33

  9. Meister, A. An enzymatic basis for a blood brain barrier? The γ-glutamyl cycle — background and considerations relating to amino acid transport in the brain. In Plum, F. (ed.)Brain Dysfunction in Neurological Disorders. Raven Press, New York, 1974, p. 273

  10. Meister, A. and Tate, S. S. Glutathione and related gamma-glutamyl compounds: biosynthesis and utilization.Annu. Rev. Biochem. 45 (1976) 559

  11. O'Daly, S. An abnormal sulphhydryl compound in urine.Ir. J. Med. Sci. 7 (1968) 578

  12. Pellefigue, F., Butler, J. D., Spielberg, S. P., Morley, D., Hollenberg, M. D., Goodman, S. I. and Schulman, J. D. Normal amino acid uptake by cultured human fibroblasts does not require γ-glutamyl transpeptidase.Biochem. Biophys. Res. Commun. 73 (1976) 997

  13. Prusiner, P. E. and Prusiner, S. B. Partial purification and kinetics of γ-glutamyl transpeptidase from bovine choroid plexus.J. Neurochem. 30 (1978a) 1253

  14. Prusiner, P. E. and Prusiner, S. B. Modulation of γ-glutamyl transpeptidase activity from bovine choroid plexus.J. Neurochem. 30 (1978b) 1262

  15. Schulman, J. D., Goodman, S. I., Mace, J. W., Patrick, A. D., Tietze, F. and Butler, E. J. Glutathionuria: inborn error of metabolism due to tissue deficiency of gamma-glutamyl transpeptidase.Biochem. Biophys. Res. Commun. 65 (1975) 68

  16. Scriver, C. R. and Rosenberg, L. E.Amino Acid Metabolism and its Disorders, W. B. Saunders, Philadelphia, 1973, p. 39

  17. Spaeth, G. L. and Barber, G. W. Prevalence of homocystinuria among the mentally retarded: evaluation of a specific screening test.Pediatrics 40 (1967) 586

  18. Tietze, F. Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: applications to mammalian and other tissues.Anal. Biochem. 27 (1969) 502

  19. Varley, H.Practical Clinical Biochemistry (4th ed.), Heinemann, London, 1967, p. 197

  20. Wilcken, B. and Turner, G. Homocystinuria in New South Wales.Arch. Dis. Child. 53 (1978) 242

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Wright, E.C., Stern, J., Ersser, R. et al. Glutathionuria: γ-Glutamyl transpeptidase deficiency. J Inherit Metab Dis 2, 3–7 (1979). https://doi.org/10.1007/BF01805554

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  • Public Health
  • Enzyme Activity
  • Internal Medicine
  • Glutathione
  • Plasma Level