Title: Identification of the major protein adduct formed in rat liver after thioacetamide administration.
Authors: Dyroff, M C; Neal, R A
Published In Cancer Res, (1981 Sep)
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.
PubMed ID: 6790164
MeSH Terms: Acetamides/administration & dosage*; Amino Acids/analysis; Animals; Chromatography, Ion Exchange; Gas Chromatography-Mass Spectrometry; Liver/drug effects*; Liver/metabolism; Lysine/analogs & derivatives; Lysine/analysis; Male; Proteins/analysis; Proteins/isolation & purification*; Rats; Thioacetamide/administration & dosage*