Enzymatic assay for glutathione.
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Biomedical subjects
Publications and source records attributed to J E Brehe.
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The effect of L-methionine-DL-sulfoximine (MSO) on renal glutathione concentration and aspartic acid transport has been studied by analyses of parts of individual freeze-dried glomeruli, early and late proximal convoluted, early and late proximal straight, and distal straight and convoluted tubules, and patches from thinlimb and papilla areas. Glutathione normally varies threefold along the kidney nephron, being highest in the convoluted and early straight proximal tubule, lowest in the distal straight tubule. Large loads of aspartate cause 20% diminution of glutathione in outer cortex, due entirely to changes in proximal tubule segments. MSO alone lowers glutathione 90% in all parts of the proximal tubule, with no change elsewhere. MSO does not affect the large increase in aspartate in proximal tubules caused by saturating aspartate loads, suggesting that glutathione is not directly involved in transport of this amino acid. Aspartate loads cause a large increase in renal glutamine, which is especially marked in the proximal straight tubule. MSO effectively blocks this increase and depresses tissue glutamine below normal levels.
Three gluconeogenic enzymes, P-pyruvate carboxykinase (PPCK), fructose-1-6 bisphosphatase (FBPase), and glucose-6-phosphatase (G6Pase) were measured in identified structures of rat nephron from 2 days before birth to maturity. In the proximal convoluted tubule, the three enzymes increased from the earliest age assayed to +14 days (PPCK, 7-fold, FBPase, 2-fold and G6Pase, 50-fold). Among the 7 defined structures that were analyzed, highest levels at all ages were in the proximal convoluted tubule with almost no activity in the distal convoluted tubule. All three enzymes had negligible activity in the neogenic zone and mesenchyme. Supported by grants from the Public Health Service (HD 03891 and NS-05221) and the American Cancer Society (P-78).