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Hemoglobingroups in green. From .Hemoglobin, also spelled haemoglobin and abbreviated Hb, is the iron-containing oxygen-transport metalloprotein in the red blood cells of the blood in vertebrates and other animals. In mammals the protein makes up about 97% of the red cell’s dry content, and around 35% of the total content . Hemoglobin transports oxygen from the lungs or gills to the rest of the body, such as to the muscles, where it releases its load of oxygen. Hemoglobin also has a variety of other gas-transport and effect-modulation duties, which vary from species to species, and may be quite diverse in invertebrates. 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 group; each heme group contains an iron atom, and this is responsible for the binding of oxygen through ion-induced dipole forces. The most common type of hemoglobin in mammals contains four such subunits, each with one heme group. In humans, each heme group is able to bind one oxygen molecule, and thus, one hemoglobin molecule can bind four oxygen molecules.Mutations in the genes for the hemoglobin protein in humans result in a group of hereditary diseases termed the hemoglobinopathies, the best known of which is sickle-cell disease. Historically in human medicine, sickle-cell disease was the first disease to be understood in its mechanism of dysfunction, completely down to the molecular level. However, not all such globin-gene mutations result in illness. These mutations are formally recognized as hemoglobin variants rather than diseases. A separate set of diseases involves underproduction of normal and sometimes abnormal hemoglobins, through problems and mutations in globin gene regulation. These diseases, which also often produce anemia, are called thalassemias.Hemoglobin is synthesized in a complex series of steps. The heme portion is synthesized in a series of steps which occur in the mitochondria and the cytosol of the immature red blood cell, while the globin protein portions of the molecule are synthesized by ribosomes in the cytosol. Production of Hb continues in the cell throughout its early development from the proerythroblast to the reticulocyte in the bone marrow. At this point, the nucleus is lost in mammalian red blood cells, but not in birds and many other species. Even after the loss of the nucleus in mammals, residual ribosomal RNA allows further synthesis of Hb until the reticulocyte loses its RNA soon after entering the vasculature . The chemical empirical formula of the most common human hemoglobin is C738H1166N812O203S2Fe, but as noted above, hemoglobins vary widely across species, and even slightly among subgroups of humans. (From the Wikpedia article Hemoglobin.) Download PDF containing detailed information. Image ResultsLoading...
BioPortfolio Ltd. offers e-mail and postal lists for Hemoglobin scientists - we have details of around 7538 individuals working on Hemoglobin . This page has been viewed 1595 times Recent Search Terms used to find this page: hemoglobin empirical formula | hemoglobin formula | hemoglobin raleigh wiki | hemoglobin formula | formula hemoglobina | blood gass transport,anemia, pdf | blood gass transport,anemia, pdf | formula of hemoglobin | Balanced management of hepatic trauma is associated with low liver-related mortality. | . Browse BioPortfolio's InDepth service - alphabetically: A B C D E F G H I J K L M N O P Q R S T U V W X Y Z or by Most Publications, recently searched for, or most viewed. Search for Hemoglobin across BioPortfolio, or for Hemoglobin Research Reports Wikipedia excerpt, where present, licenced under the GNU Free Documentation License. Resources from the NCBI applied. Selected MeSH subject headings created and maintained by the US NLM are used in conjunction with additional keywords. 2006-2008 MeSH. Thumbshots from Thumbshots.org | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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