A liver enzyme that conjugates sulfobromophthalein sodium with glutathione.
نویسندگان
چکیده
In the past few years, considerable evidence has been presented indicating that sulfobromophthalein sodium (BSP) is metabolized in the liver (1-6). Recently, we have demonstrated that the major pathway of BSP metabolism in man and in the rat involves conjugation of BSP with.the tripeptide glutathione (5). Similar results have been obtained by Javitt and his associates in the dog (6). Grodsky, Carbone and Fanska concluded "that BSP is excreted at least in part as a mercaptide with cysteine or the peptide glutathione," in man (4). These latter authors are not certain about the presence of glutathione, however, since they feel that glycine and glutamic acid are possible contaminants of the BSP metabolites. The results of the present investigation disclosed three critical features of hepatic BSP metabolism; first, an enzyme is described, identified in liver, which catalyzes the conjugation of BSP and glutathione; second, glutathione is shown to be the preferred substrate for the enzyme; finally, it is demonstrated that 1 mole of bromide ion is released from BSP for each mole of BSP-glutathione formed.
منابع مشابه
The intrahepatic conjugation of sulfobromophthalein and glutathione in the dog.
In 1950 Brauer, Krebs and Pessotti (1) reported that S35-labeled sodium phenoltetrabromophthalein disulfonate (more commonly known as sulfobromophthalein, Bromsulfalein or BSP) may be recovered from the bile of the dog, during constant intravenous infusion, in four fractions which are separable by column chromatography. Similar fractions, accounting for the bulk of BSP excreted and having absor...
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عنوان ژورنال:
- The Journal of clinical investigation
دوره 40 شماره
صفحات -
تاریخ انتشار 1961