been released from erythrocytes, thereby inhibiting its oxidative activity. During this process, Haptoglobin sequesters the iron within Hemoglobin, preventing iron-utilizing bacteria from benefitting from hemolysis. This function suggests that Haptoglobin concentrations may increase in response to inflammation. The resulting Haptoglobin-Hemoglobin complex is then removed by the reticulo-endothelial system. Due to cleavage of a common precursor protein during protein synthesis, Haptoglobin consists of two α and two β chains, connected by disulfide bridges.
