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The structural characterisation of the adducts formed by in vitro interaction of hemoglobin (Hb) with 1,2,3,4‐diepoxybutane (DEB), the most reactive 1,3‐butadiene (BD) metabolite, was obtained by liquid chromatography/electrospray ionisation mass spectrometry (LC/ES‐MS) analysis of modified tryptic peptides of human hemoglobin chains. The reactive sites of human hemoglobin towards DEB and its hydroxylated derivatives (trihydroxybutyl (THB)‐derivatives) were identified through the characterisation of alkylated tryptic peptides by matrix‐assisted laser desorption/ionisation tandem mass spectrometry (MALDI‐MS/MS). Based on this characterisation, a procedure was set up to measure the Hb‐adducts of THB‐derivatives by isotope dilution mass spectrometry with the use of a deuterated peptide standard. The results obtained here could permit optimisation of molecular dosimetry of BD‐adducts, and extension …