By N. Tateishi, T. Higashi (auth.), Professor Dr. Helmut Sies, Dozent Dr. Albrecht Wendel (eds.)

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Res. Commun. ~, 68-74 (1975) 12. : Enzymatic method for quantitative determination of nanogram amounts of total and oxidized glutathione: Applications to mammalian blood and other tissues. Anal. Biochem. ~, 502-522 (1969) 13. : On the role of y-glutamyltransferase in renal tubular amino acid reabsorption. In: Renal metabolism in relation to renal function. C. ), pp. 426-436. Bern-Stuttgart-Vienna: Hans Huber Publishers 1976 14. : Enzymatic assay for glutathione. Anal. Biochem. 2±, 189-197 (1976) 15.

According to this interpretation, the y-glutamyl moiety is the carrier and the y-glutamyl amino acid is translocated into the cell. Within the cell, the amino acid is released from its y-glutamyl carrier by the action of y-glutamyl cyclotransferase. The energy-requiring steps of the cycle include those involved in the resynthesis of glutathione and the conversion of 5oxoproline to glutamate. It should be emphasized that we have not proposed that the y-glutamyl cycle mediates transport of all amino acids, nor have we suggested that it is the only amino acid transport mechanism.

1 G = 80 - h DON Fig. 2 Fig. 1. Inactivation of fetal hepatic y-glutamyltranspeptidase and accumulation of glutathione in fetal liver by treatment with DON. DON (25 ~mol) or saline was injected to pregnant mice intravenously on gestational day 17, 18, or 19 and the animals were killed 4 h after injection. y-glutamyltranspeptidase activity and glutathione concentration were examined in fetal liver. Three to five mothers were used for each experiment. The figures for saline-injected group was taken as 100% Fig.

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