Identification of the major protein adduct formed in rat liver after thioacetamide administration.
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TL;DR
The in vivo covalent binding of the hepatocarcinogen thioacetamide to rat liver protein has been examined and additional studies indicated the structure of this adduct was N-epsilon-acetyllysine.
Abstract
The in vivo covalent binding of the hepatocarcinogen thioacetamide to rat liver protein has been examined. Following administration of 3H- or 14C-labeled thioacetamide, the modified amino acids present in the hepatic cytosolic proteins were isolated by enzymatic digestion and ion-exchange chromatography. Approximately 70% of the radioactivity covalently bound to cytosolic protein was recovered in a compound which upon acid hydrolysis yielded lysine and radiolabeled acetate. Additional studies indicated the structure of this adduct was N-epsilon-acetyllysine.