Isolation of alkylated rat hemoglobin adducts using metal-affinity chromatography

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-1...

Full description

Saved in:
Bibliographic Details
Published in:Russian journal of bioorganic chemistry 2012, Vol.38 (1), p.41-45
Main Authors: Dubrovskii, Ya. A., Gladilovich, V. D., Krasnov, I. A., Podolskaya, E. P., Murashko, E. A., Babakov, V. N.
Format: Article
Language:English
Subjects:
Biochemistry
Biomedical and Life Sciences
Biomedicine
Bioorganic Chemistry
Life Sciences
Organic Chemistry
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:1068-1620
1608-330X
DOI:10.1134/S1068162012010050