Abstract
Glossoscolex paulistus hemoglobin (HbGp) has a molecular mass of 3.6 MDa, determined by analytical ultracentrifugation (AUC). HbGp presents high oligomeric stability, resistance to oxidation and affinity to oxygen binding. The quaternary structure of this macromolecule consists of 144 globin chains, and 36 additional chains, lacking the heme group, named linkers, organized in a double-lay…