Hemoglobin

Hemoglobin A is the major hemoglobin found in adult humans, comprising about 90 percent of their total hemoglobin (Devlin 1030). Two to three percent of adult hemoglobin is hemoglobin A2, which has two ? chains and two ? chains, which differ in amino acid sequence to ? chains and are under independent genetic control (Devlin 1030). There are several modified version of hemoglobin A in the human, most with sugars such as glucose, glucose-6-phosphate or fructose 1,6-bisphosphate bound to them. The most significant is hemoglob

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: the high levels of oxygen in the lungs encourages the release of carbon dioxide and oxygen uptake, while the reverse is true in the tissues (Devlin 1026). Hemoglobin has a short lifespan in plasma, rapidly dissociating into ?? dimers, which are bound by a plasma protein known as haptoglobin and removed from the circulation (Devlin 1026). Hemoglobin within erythrocytes has a lifespan of approximately 120 days - the lifespan of an erythrocyte (Berkow, Beers and Fletcher 746). Abnormal forms of hemoglobin in humans cause anemia because they cannot carry sufficient oxygen to the tissues, and diseases such as sickle cell anemia, hemoglobin C disease, hemoglobin S-C (a combination of sickle cell disease and hemoglobin C disease) and hemoglobin E disease(Berkow, Beers and Fletcher 751). These disease are found primarily in Blacks. and hemoglobin E disease is also found in some Southeast Asians (Berkow, Beers and Fletcher 751). These hemoglobinopathies may involve the substitution of an amino acid in one of the polypeptide chains, or may be caused by an omission of an amino acid from a polypeptide chain of the hemoglobin (Devlin 1030). Thalassemias are a group of genetic disease caused by the production of unbalanced numbers of
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