Ceruloplasmin, the major copper-carrying protein in the blood plays a role in iron metabolism. It prevents the oxidation that leads to the forming of oxidation from Fe2+ (ferrous iron) into Fe3+ (ferric iron) by exhibiting a copper-dependent oxidase activity, causing mutations in the ceruloplasmin gene cause of iron overload in the brain, liver, pancreas, and retina.
Ferritin, the protein produced by almost all living organisms, acts as a component to fight against iron deficiency and iron overload, keep in a soluble and non-toxic form and transport it to the body needs, including organs. It enhances the immune system in the presence of an infection or cancer and prevent the infectious agent attempts to bind iron to become free radicals by migrating from the plasma to within cells.
Lactoferrin, a multifunctional protein of the transferrin family, is one of the components of the immune system of the body by fighting against foreign invasion of bacteria and virus and lipid oxidation by inhibiting oxidation in a concentration-dependent manner even at concentrations beyond its capacity.
Metallotheinein, a family of cysteine-rich, low molecular weight proteins helps to bind both physiological heavy metals through the organosulfur compound of its cysteine residues. It also captures harmful superoxide and hydroxyl radicals by liberating the metal ions which were bound to cysteine.
Transferrin is a glycoprotein that binds iron very tightly but reversibly. It enhance the immune system in fighting against infection, inflammation by creating an environment low in free iron that impedes bacteria survival and cell oxidation.
Hemoglobin is the protein molecule in red blood cells that enhances the carrying of oxygen from the lungs to the body's tissues and return CO2 from the tissues to the lungs.
During oxidate stress, the cell membrane is protected by intraerythrocytic hemoglobin from the forming of free radical.
Myoglobin is an iron- and oxygen-binding protein found in the muscle tissue of vertebrates. The binding of oxygen by myoglobin is unaffected by the oxidation or chain of oxidative reaction in the surrounding tissue, thus reducing the free radicals damage caused by oxidate stress.