Hemoglobin failure, or abnormal hemoglobin (such as that of sickle-cell disease). The ability of each hemoglobin molecule to carry oxygen is normally modified by altered blood pH or CO, causing an altered oxygen–hemoglobin dissociation curve. However, it can also be pathologically altered in, e.g., carbon monoxide poisoning. Decrease of hemoglobin, with or without an absolute decrease of red blood cells, leads to symptoms of anemia. Anemia has many different causes, although iron deficiency and its resultant iron deficiency anemia are the most common causes in the Western world. As absence of iron decreases heme synthesis, red blood cells in iron deficiency
Blood hemoglobin with a much higher affinity for oxygen (hemoglobin F) to function under these conditions. CO is carried in blood in three different ways. (The exact percentages vary depending whether it is arterial or venous blood). Most of it (about 70%) is converted to bicarbonate ions by the enzyme carbonic anhydrase in the red blood cells by the reaction CO + HO → HCO → H + ; about 7% is dissolved in the plasma; and about 23% is bound to hemoglobin as carbamino compounds. Hemoglobin, the main oxygen-carrying molecule in red blood cells, carries both oxygen and carbon dioxide.