<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Peng L</submitter><funding>NCI NIH HHS</funding><pagination>267-78</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4277649</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>103</volume><pubmed_abstract>Heterocyclic aromatic amines (HAAs) are carcinogens formed during the cooking of meats or arise in tobacco smoke. The genotoxic N-oxidized metabolites of HAAs bind to Cys residues of proteins to form arylsulfinamide adducts. However, these adducts are unstable and undergo hydrolysis during enzymatic digestion, and thus have been precluded as biomarkers of exposure to HAAs. Arylsulfinamide adducts of HAAs can undergo oxidation to form stable arylsulfonamide linkages, which are chemically stable and amenable for analysis. 2-Amino-1-methyl-6-phenylimidazo[4,5-b]pyridine (PhIP) is a carcinogen present in cooked meat. We established a quantitative MS-based method to measure the sulfinamide adduct of PhIP formed at the cysteine(34) (Cys(34)) residue of human serum albumin (SA), following chemica</pubmed_abstract><journal>Journal of proteomics</journal><pubmed_title>Optimizing proteolytic digestion conditions for the analysis of serum albumin adducts of 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine, a potential human carcinogen formed in cooked meat.</pubmed_title><pmcid>PMC4277649</pmcid><funding_grant_id>R01 CA122320</funding_grant_id><funding_grant_id>P30 CA077598</funding_grant_id><pubmed_authors>Turesky RJ</pubmed_authors><pubmed_authors>Peng L</pubmed_authors></additional><is_claimable>false</is_claimable><name>Optimizing proteolytic digestion conditions for the analysis of serum albumin adducts of 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine, a potential human carcinogen formed in cooked meat.</name><description>Heterocyclic aromatic amines (HAAs) are carcinogens formed during the cooking of meats or arise in tobacco smoke. The genotoxic N-oxidized metabolites of HAAs bind to Cys residues of proteins to form arylsulfinamide adducts. However, these adducts are unstable and undergo hydrolysis during enzymatic digestion, and thus have been precluded as biomarkers of exposure to HAAs. Arylsulfinamide adducts of HAAs can undergo oxidation to form stable arylsulfonamide linkages, which are chemically stable and amenable for analysis. 2-Amino-1-methyl-6-phenylimidazo[4,5-b]pyridine (PhIP) is a carcinogen present in cooked meat. We established a quantitative MS-based method to measure the sulfinamide adduct of PhIP formed at the cysteine(34) (Cys(34)) residue of human serum albumin (SA), following chemica</description><dates><release>2014-01-01T00:00:00Z</release><publication>2014 May</publication><modification>2025-05-29T21:08:01.202Z</modification><creation>2025-05-29T21:08:01.202Z</creation></dates><accession>S-EPMC4277649</accession><cross_references><pubmed>24698664</pubmed><doi>10.1016/j.jprot.2014.03.023</doi></cross_references></HashMap>