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| - N-Terminal Adducts of Bovine Hemoglobin withGlutaraldehyde in a Hemoglobin-Based OxygenCarrier
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| - Hemoglobin-based oxygen carriers (HBOCs) are beingdeveloped for the medical field, but because they couldincrease an athlete's performance, they are misappliedfor doping purposes. We previously presented a screeningmethod to detect Oxyglobin (Biopure Corp.) and PolyHeme (Northfield Laboratories Inc.) in serum samplesusing total acid hydrolysis followed by electrospray massspectrometry analyses. An alternative mass spectrometricmethod involving enzymatic hydrolysis is here presented.Digestion of Oxyglobin by endoproteinase Glu-C and LC/MS analyses of the mixture allowed the detection ofunique peptidic fragments in comparison with a bovinehemoglobin digest. Tandem mass spectrometry experiments of these peptide ions were performed, and twospecific species were actually identified as the N-terminalenzymatic fragment of the β chain carrying two differentmodifications. Sequential MS3 experiments using an iontrap mass spectrometer permitted us to locate the chemical modification by the glutaraldehyde on the NH2-terminal group and to propose a structure for the modifiedpeptides. In another set of experiments, screening of thesetwo diagnostic ions into Oxyglobin-spiked serums usingprecursor ion scan mode in a triple quadrupole instrument allowed the detection of this HBOC with a detectionlimit of 2 g L-1.
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