LP32067-8

Hemoglobin

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Descriptions

Hemoglobin or haemoglobin [frequently abbreviated as Hb ] is the iron -containing oxygen -transport metalloprotein in the red cells of the blood in mammals and other animals. Hemoglobin in vertebrates transports oxygen from the lungs to the rest of the body, such as to the muscles, where it releases the oxygen load. Hemoglobin also has a variety of other gas-transport and effect-modulation duties, which vary from species to species, and which in invertebrates may be quite diverse. The name hemoglobin is the concatenation of heme and globin, reflecting the fact that each subunit of hemoglobin is a globular protein with an embedded heme (or haem) group; each heme group contains an iron atom, and this is responsible for the binding of oxygen. The most common types of hemoglobin contains four such subunits, each with one heme group. Copyright Text is available under the Creative Commons Attribution/Share-Alike License. See http://creativecommons.org/licenses/by-sa/3.0/ for details. Source: Wikipedia , Hemoglobin (Wikipedia)

Hemoglobin (Hb or Hgb) is a protein in red blood cells that is responsible for transporting oxygen from the lungs to the body and transporting carbon dioxide back to the lungs. It is composed of two alpha subunits and two beta subunits non-covalently bonded.
Hemoglobin levels in the blood must be maintained to guarantee tissue oxygenation. A low concentration of hemoglobin is called anemia and can be caused either by a decreased number of erythrocytes (RBCs/red cells) in the blood or hyperhydration of the body. An increased concentration of hemoglobin can be caused either by a increased number of RBCs in the blood or dehydration of the body. [NCBI Books:NBK259] PMID: 20923558 Source: Regenstrief LOINC

Hemoglobin is a protein inside red blood cells that transports oxygen throughout the body. It is made up of two alpha chains and two beta chains with a ring-shaped heme group that contains an atom of iron. The oxygen is picked up in the alveoli by the hemoglobin protein and binds reversibly to the iron atom. At the same time, carbon dioxide that was picked up in the tissues of the body is released into the lungs and exhaled. Hemoglobin variation is seen when the structure of the protein is altered due to a mutation such as in Hemoglobin S which causes sickle cell anemia. Hemoglobin variation can also result when there is a mismatch in the number of alpha and beta chains which leads to thalassemia.[http://pdb101.rcsb.org/motm/41] Source: Regenstrief LOINC

Basic Part Properties

Part Name

Hemoglobin

Part Display Name

Hemoglobin

Part Type

Divisors (Divisors only)

Created On

2003-09-03

Construct for LOINC Short Name

Hgb

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