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| - Simple Identification of A Cross-LinkedHemoglobin by Tandem Mass Spectrometry inHuman Serum
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| - Hemoglobin-based oxygen therapeutics are prepared byreaction of hemoglobin with cross-linking molecules andare utilized as blood substitutes. They can be used asdoping agents to increase the oxygen-carrying capacity ofhemoglobin. We have compared a glutaraldehyde-polymerized bovine hemoglobin (Oxyglobin, Biopure Corp.) withnatural bovine hemoglobin by mass spectrometry in orderto detect specific fragment ions of the cross-linked proteinfor further potential applications in doping control ofhuman blood samples. HCl acid (6 N) hydrolysis wasperformed in parallel on both proteins. Hydrolysates werethen analyzed by direct infusion electrospray mass spectrometry (ESIMS) using a triple quadrupole mass spectrometer. Confirmation and precision were obtained byLC−ESIMSn experiments performed on an ion trap massspectrometer. Chromatographic and mass spectrometrydata allowed detection of two potential Oxyglobin-specificionsm/z 299 and 399that were shown to lose a 159u neutral fragment under collision-induced dissociationconditions. Thus, monitoring of constant neutral loss of159 u on acid hydrolysates of human serum samplesspiked with different amounts of Oxyglobin has provedto be an efficient screening method to specifically detectand identify Oxyglobin. LC−MS of the spiked serumsample hydrolysates enabled detection of Oxyglobin at adetection limit of 4 g·L-1.
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