Characterization of Sulfur Mustard Induced Structural Modifications in Human Hemoglobin by Liquid Chromatography-Tandem Mass Spectrometry
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- 作者：Daan Noort ; Elwin R. Verheij ; Albert G. Hulst ; Leo P. A. de Jong ; and Hendrik P. Benschop
- 刊名：Chemical Research in Toxicology
- 出版年：1996
- 出版时间：June 1996
- 年：1996
- 卷：9
- 期：4
- 页码：781 - 787
- 全文大小：192K
- 年卷期：v.9,no.4(June 1996)
- ISSN：1520-5010
文摘
In this paper we describe the use of tandem mass spectrometry toidentify modified sites inhuman hemoglobin after in vitro exposure tobis(2-chloroethyl) sulfide (sulfur mustard).Globinisolated from human whole blood which had been exposed to sulfurmustard was degradedwith trypsin, and the digests were analyzed by micro LC/MS.Alkylated tryptic fragments(
-T1, -T4, -T6, -T9, 
-T1, -T9, -T10, -T11, and-T10-S-S--T12) could be tentativelyassigned upon comparison with a digest from nonexposed globin.Subsequent tandem massspectrometry of these peptides allowed unambiguous assignment of 5specific modifiedresidues: -Val-1, -His-20, -Val-1, -His-77, and-His-97. The results demonstrate theusefulness of microbore LC in combination with tandem mass spectrometryfor the structuraldetermination of chemically modified peptides andproteins.
-T1, -T4, -T6, -T9, -T1, -T9, -T10, -T11, and-T10-S-S--T12) could be tentativelyassigned upon comparison with a digest from nonexposed globin.Subsequent tandem massspectrometry of these peptides allowed unambiguous assignment of 5specific modifiedresidues: -Val-1, -His-20, -Val-1, -His-77, and-His-97. The results demonstrate theusefulness of microbore LC in combination with tandem mass spectrometryfor the structuraldetermination of chemically modified peptides andproteins.