Characterization of N-terminal formaldehyde adducts to hemoglobin

被引：8
作者：
Ospina, Maria [1 ]
Costin, Alina [1 ]
Barry, Adrienne K. [1 ]
Vesper, Hubert W. [1 ]
机构：
[1] Ctr Dis Control & Prevent, Div Sci Lab, Natl Ctr Environm Hlth, Atlanta, GA 30341 USA
来源：
RAPID COMMUNICATIONS IN MASS SPECTROMETRY | 2011年 / 25卷 / 08期
关键词：
STRUCTURAL-CHARACTERIZATION; ACETALDEHYDE ADDUCTS; INHALATION EXPOSURE; MASS-SPECTROMETRY; PROTEIN ADDUCTS; MODEL PEPTIDES; GLOBIN ADDUCTS; IN-VITRO; IDENTIFICATION; ACRYLAMIDE;
D O I：
10.1002/rcm.4954
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
A procedure to prepare and purify adducts of formaldehyde ( FA) to the N-terminus of peptides was developed. FA-VHLTPEEK and FA-VLSPADK were produced with purities >95% upon incubation of the peptides with FA in phosphate-buffered saline (PBS) at a pH level of 7.4. The peptides were purified by preparative liquid chromatography and were characterized by their retention times in liquid chromatography, their fragmentation patterns obtained by tandem mass spectrometry, and their accurate mass and nuclear magnetic resonance measurements. This is the first time an imidazolidone-type structure has been reported for FA adducts. The same peptides were identified in tryptic digests of human hemoglobin incubated with FA at physiological conditions and in human hemoglobin specimens. These peptides are suitable for use as calibrators for the quantitative assessment of internal exposure to FA. Published in 2011 by John Wiley & Sons, Ltd.
引用
收藏
页码：1043 / 1050
页数：8
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