This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Dyroff, M. C. Articles by Neal, R. A. Search for Related Content PubMed PubMed Citation Articles by Dyroff, M. C. Articles by Neal, R. A.

Identification of the Major Protein Adduct Formed in Rat Liver after Thioacetamide Administration¹

Center in Environmental Toxicology, Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, Tennessee 37232

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--acetyllysine.

¹ This work was supported by Grants ES 00075 and ES 00267.

² Recipient of Grant ES 07028.

³ To whom requests for reprints should be addressed.

Received 3/20/81. Accepted 6/11/81.