GLUTATHIONE-RELATED ENZYME-ACTIVITIES IN HUMAN FETAL ADRENAL, LIVER, AND KIDNEY

AIM: To understand the capacity of fetal adrenal to catalyze reaction metabolites. METHODS: Subcellular fractions were prepared by different ial centrifugation in fetal adrenal and liver. Glutathione (GSH)-trans ferase, reductase, and peroxidase were measured. RESULTS: The mean val ues (mu mol.min(-1)/g protein) of GSH-transferase activities in adrena l microsome (112 +/- 34), mitochondria (62 +/- 5), and cytosol (191 +/ - 89) were 373 %, 270 %, and 167 %, respectively, higher than those in the corresponding fractions of fetal liver. Adrenal microsomal GSH-tr ansferase was positively correlated with adrenal microsomal P-450 (r = 0.821, P < 0.01), and with adrenal microsomal aminopyrine N-demethyla se (r = 0.829, P < 0.01). The GSH reductase contents (mu mol.min(-1)/g protein) in adrenal mitochondria (24 +/- 14), and in S-9 (36 +/- 15) were almost 5 times higher, compared with that in liver. Selenium-depe ndent GSH peroxidase was present in all the adrenal. CONCLUSION: Fetal adrenal, with greater capacities than those of liver in detoxifying r eaction, may act as a drug-metabolizing organ during development.