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Characterization of N‐terminal formaldehyde adducts to hemoglobin
Author(s) -
Ospina Maria,
Costin Alina,
Barry Adrienne K.,
Vesper Hubert W.
Publication year - 2011
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.4954
Subject(s) - chemistry , chromatography , adduct , hemoglobin , tandem mass spectrometry , fragmentation (computing) , formaldehyde , mass spectrometry , high performance liquid chromatography , biochemistry , organic chemistry , computer science , operating system
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.