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Role of mixed-function oxidases and non-protein sulfhydryl contentent in [14C]-2-chloro-4-acetotoluidide binding to liver and kidney in starlings

โœ Scribed by Shri N. Giri; David M. Siegel


Publisher
John Wiley and Sons
Year
1990
Tongue
English
Weight
924 KB
Volume
10
Category
Article
ISSN
0260-437X

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โœฆ Synopsis


The compound 2-chloro-4-acetotoluididc (CAT) is highly toxic to many avian species, including the starling. In our earlier work, we demonstrated the covalent binding of radioactivity from [14C]-CAT to liver and kidneys of the starling. In the present study, the effects of inducers of mixed-function oxidase (MFO) and non-protein sulfhydryl (NPSH) depletor on the total and covalent binding of [14C]-CAT radioactivity to liver and kidney of the starling were examined. The total and covalently bound radioactivity from [IJC]-CAT to liver and kidney were decreased significantly in the starling pretreated with the MFO inducer, 3methylcholanthrene. However, pretreatment with phenobarbital, another inducer of MFO, had no effect. Pretreatment with the inhibitor of MFO, SKF 525-A, reduced the covalent binding of [14C]-CAT radioactivity to liver but not to kidney. There was no reduction in the NPSH content of liver or kidney following intravenous administration of CAT (3.5 mg kg-'). Reduction of NPSH levels in the liver or kidney following treatment with diethyl maleate caused a significant increase in the covalent binding of [14C]-CAT to kidney but not to liver.


๐Ÿ“œ SIMILAR VOLUMES


Characterization of covalent binding of
โœ Giri, Shri N. ;Siegel, David M. ๐Ÿ“‚ Article ๐Ÿ“… 1991 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 794 KB

In this study, we have characterized the covalent binding of ['4C1-2-chloro-4-acetotolui- dide (CAT) radioactivity to microsomes of starling liver and kidney. The maximal velocity ( V , , , ) of covalent binding and apparent Michaelis constant (K,) for both tissues were similar. The V , , for liver