{"title":"谷胱甘肽衍生物在大鼠肾脏中的降解。","authors":"A Wendel, H Heinle, S Silbernagl","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Single proximal rat kidney tubules and Henle loops were microperfused with labelled S-substituted glutathione derivatives which are physiological mercapturic acid precursors. S-methyl-glutathione as well as the non-permeating bromo-sulfaleinglutathione adduct were degraded in the proximal convolution with a half-life of about 3.5 sec. The findings demonstrate that the brush-border membrane-bound renal gamma-glutamyl transpeptidase acts on luminal substrates and is involved in mercapturic acid synthesis and splitting of extracellular glutathione.</p>","PeriodicalId":72742,"journal":{"name":"Current problems in clinical biochemistry","volume":"8 ","pages":"73-84"},"PeriodicalIF":0.0000,"publicationDate":"1977-10-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"The degradation of glutathione derivatives in the rat kidney.\",\"authors\":\"A Wendel, H Heinle, S Silbernagl\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Single proximal rat kidney tubules and Henle loops were microperfused with labelled S-substituted glutathione derivatives which are physiological mercapturic acid precursors. S-methyl-glutathione as well as the non-permeating bromo-sulfaleinglutathione adduct were degraded in the proximal convolution with a half-life of about 3.5 sec. The findings demonstrate that the brush-border membrane-bound renal gamma-glutamyl transpeptidase acts on luminal substrates and is involved in mercapturic acid synthesis and splitting of extracellular glutathione.</p>\",\"PeriodicalId\":72742,\"journal\":{\"name\":\"Current problems in clinical biochemistry\",\"volume\":\"8 \",\"pages\":\"73-84\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1977-10-23\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Current problems in clinical biochemistry\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Current problems in clinical biochemistry","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
The degradation of glutathione derivatives in the rat kidney.
Single proximal rat kidney tubules and Henle loops were microperfused with labelled S-substituted glutathione derivatives which are physiological mercapturic acid precursors. S-methyl-glutathione as well as the non-permeating bromo-sulfaleinglutathione adduct were degraded in the proximal convolution with a half-life of about 3.5 sec. The findings demonstrate that the brush-border membrane-bound renal gamma-glutamyl transpeptidase acts on luminal substrates and is involved in mercapturic acid synthesis and splitting of extracellular glutathione.