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.
Mutations in the genes for the hemoglobin protein in humans result in a group of hereditary diseases termed the hemoglobinopathies, the most common members of which are sickle-cell disease and thalassemia. Historically in human medicine, hemaglobinopathies were the first diseases to be understood in mechanism of dysfunction, down to the molecular level.
Hemoglobin is synthesized in the mitochondria of the immature red blood cell throughout its early development from the proerythroblast to the reticulocyte in the bone marrow, when the nucleus has been lost. Even after the loss of the nucleus, residual ribosomal RNA allow further synthesis of Hb until the reticulocyte loses its RNA on entering the vasculature. Hemoglobin is chemically represented by (C2952H4664N812O832S8Fe4).
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.
Mutations in the genes for the hemoglobin protein in humans result in a group of hereditary diseases termed the hemoglobinopathies, the most common members of which are sickle-cell disease and thalassemia. Historically in human medicine, hemaglobinopathies were the first diseases to be understood in mechanism of dysfunction, down to the molecular level.
Hemoglobin is synthesized in the mitochondria of the immature red blood cell throughout its early development from the proerythroblast to the reticulocyte in the bone marrow, when the nucleus has been lost. Even after the loss of the nucleus, residual ribosomal RNA allow further synthesis of Hb until the reticulocyte loses its RNA on entering the vasculature. Hemoglobin is chemically represented by (C2952H4664N812O832S8Fe4).
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