Research output: Contribution to journal › Article › peer-review
Metal-affinity chromatography with Cu2+ containing sorbent was used for separation of globin peptides alkylated by sulfur mustard. It was shown that matrix-assisted laser desorption/ionization time-offlight mass spectrometry allowed isolating peptides alkylated by sulfur mustard (HD) at cysteine-126, -94 and glutamic acid-27 with MH+ of 1444.62, 1561.66, 1676.78 Da, respectively, from rat globin tryptic digest incubated with 60 μM of HD. An alkylated peptide with MH+ of 1444.63 Da was isolated from globin hydrolyzate incubated with 3 μM of HD.
| Original language | English |
|---|---|
| Pages (from-to) | 41-45 |
| Number of pages | 5 |
| Journal | Russian Journal of Bioorganic Chemistry |
| Volume | 38 |
| Issue number | 1 |
| DOIs | |
| State | Published - 1 Jan 2012 |
ID: 36362513