Characterization of large molecular size Hemoglobin-Based Oxygen Carriers by high-mass MALDI MS

摘要

Oxidation of Hb induces specific structural changes leading to multimeric Hb species similar to HBOCs and significantly impair physiologic Hb scavenging. Poly-(alpha)XLHb and (alpha)XLHb binds to Hp 1-1 much weaker, compared to HbA0. The data suggests that unmodified alpha-chains of Hb are crucial for the high affinity interaction with Hp. These results provide valuable information on mass and stoichiometry of haptoglobin binding, which contributes to the overall understanding of specific toxicity and clearance of HBOCs and might help in rational design of HBOCs with limited Hb toxicity.