Hemoglobin
Hemoglobin or haemoglobin (frequently abbreviated as Hb, {{PDB|1A3N}}) is the iron-containing oxygen-transport metalloprotein in the red cells of the blood in mammals and other animals. The molecule consists of globin, the apoprotein, and four heme (or haem) groups, which are organic molecules with an iron atom in each.
Degradation of hemoglobin
When red cells reach the end of their life, they are broken down, and the
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hemoglobin molecule broken up and the iron recycled. When the porphyrin ring
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is broken up, the fragments are normally secreted in the bile by the liver. The major final product of heme degradation is bilirubin. Increased levels of this chemical are detected in the blood if red cells are being destroyed more rapidly than usual. Improperly degraded hemoglobin protein or hemoglobin that has been released from the blood cells can clog small blood vessels especially the delicate blood filtering vessels of the kidneys, causing kidney damage.
Related Topics:
Bile - Liver - Bilirubin - Kidney
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~ Table of Content ~
| ► | Introduction |
| ► | Structure |
| ► | Binding of ligands |
| ► | Degradation of hemoglobin |
| ► | Other biological oxygen-binding proteins |
| ► | Role in disease |
| ► | Diagnostic use |
| ► | See also |
| ► | External links |
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