**1. Introduction**

Iron is a vital trace element for all living cells. Despite the fact, this key metal is essential, and maintaining its biological balance in an organism is far more important than any other trace element except copper [1]. Excess iron, due to its catalysis of one electron redox chemistry, plays a key role in the formation of toxic oxygen radicals. Indeed, this is readily observed in diseases such as thalassemia and sickle cell anemia. This potentially hazardous combination of oxygen and iron within the erythrocyte is kept in check by several endogenous mechanisms. Intra-erythrocytic free iron can be a potential hazard to form free radicals in the presence of reduced glutathione. Free radicals can have an adverse effect on hemoglobin by oxidative damage [2]. Glutathione (GSH) is thought to be a prooxidant in iron-mediated hemoglobin oxidation, which can be prevented by iron chelation. Researchers picked two *in vitro* hemoglobin models to test this theory. RBC hemolysate, which is essentially distilled water lysed RBC, and crude pure hemoglobin (Hb-A) eluted off a Sephadex desalting column.
