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Effect of dithiocarb and dimethyl sulfoxide on irreversible binding of 14C-bromobenzene to rat liver microsomal protein.

作者信息

Younes M, Siegers C P, Filser J G

出版信息

Arch Toxicol. 1979 Sep;42(4):289-93. doi: 10.1007/BF00334843.

Abstract

The irreversible binding of [14C]-bromobenzene to rat liver microsomal protein in vitro was inhibited by dithiocarb and DMSO. Dithiocarb suppressed this binding in a time- and concentration-dependent manner (I50 = 4.5 10(-5) M). DMSO reduced the degree of covalent binding by 61% from 5 x 10(-5) M to 8 x 10(-4) M. Dithiocarb was also effective in inhibiting irreversible binding of bromobenzene to liver protein in vivo. Our results are consistent with the hypothesis that dithiocarb exerts its antihepatotoxic efficacy by depressing microsomal mixed-function oxidase activity.

摘要

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本文引用的文献

1
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Irreversible protein binding of metabolites of ethynylestradiol in vivo and in vitro.
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Irreversible protein binding of 14C-imipramine in rats in vivo.
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In vivo and in vitro effects of thiuram disulfides and dithiocarbamates on hepatic microsomal drug metabolism in the rat.
Toxicol Appl Pharmacol. 1979 Apr;48(2):343-50. doi: 10.1016/0041-008x(79)90041-3.
9
Effect of dithiocarb on metabolism and covalent binding of carbon tetrachloride.
Toxicol Appl Pharmacol. 1978 Dec;46(3):709-16. doi: 10.1016/0041-008x(78)90316-2.
10
The antihepatotoxic activity of dithiocarb as compared with six other thio compounds in mice.
Arch Toxicol. 1978 Oct 13;41(1):79-88. doi: 10.1007/BF00351772.

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