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Updated: Jun 3, 2026

Measurement of Heme Synthesis Levels in Mammalian Cells
Published on: July 9, 2015
Characterization of N-terminal formaldehyde adducts to hemoglobin
Maria Ospina1, Alina Costin, Adrienne K Barry
1Division of Laboratory Sciences, National Center for Environmental Health, Centers for Disease Control and Prevention, Atlanta, GA 30341, USA. MOspina@cdc.gov
Abstract:
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.
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