Isolation of alkylated rat hemoglobin adducts using metal-affinity chromatography

摘要

Metal-affinity chromatography with Cu ~(2+) containing sorbent was used for separation of globin peptides alkylated by sulfur mustard. It was shown that matrix-assisted laser desorption/ionization time-of-flight mass spectrometry allowed isolating peptides alkylated by sulfur mustard (HD) at cysteine-126, -94 and glutamic acid-27 with M H ~+ of 1444.62, 1561.66, 1676.78 Da, respectively, from rat globin tryptic digest incubated with 60 μM of HD. An alkylated peptide with M H ~+ of 1444.63 Da was isolated from globin hydrolyzate incubated with 3 μM of HD.