Abstract
The hydroxamic acid of 3'-hydroxyacetanilide (AMAP) was synthesized to test the hypothesis that different reactive metabolites of AMAP and acetaminophen account for similarities in covalent binding of the two positional isomers to hepatic proteins, but for differences in their ability to cause hepatotoxicity. N-OH-AMAP was found to be a relatively stable hydroxamic acid, but it was not detected as a metabolite of AMAP formed in vitro by mouse liver microsomes or in urine of mice administered AMAP. Therefore, metabolites other than N-OH-AMAP must be responsible for covalent binding observed with AMAP to mouse liver proteins.
DMD articles become freely available 12 months after publication, and remain freely available for 5 years.Non-open access articles that fall outside this five year window are available only to institutional subscribers and current ASPET members, or through the article purchase feature at the bottom of the page.
|
Log in using your username and password
Purchase access
You may purchase access to this article. This will require you to create an account if you don't already have one.