News tagged with haemoglobin
Hemoglobin
Hemoglobin (English pronunciation: /hiːməˈɡloʊbɪn/; also rendered as haemoglobin and abbreviated Hb or Hgb) is the iron-containing oxygen-transport metalloprotein in the red blood cells of all vertebrates, with the exception of the fish family Channichthyidae, as well as the tissues of some invertebrates. Hemoglobin in the blood carries oxygen from the respiratory organs (lungs or gills) to the rest of the body (i.e., the tissues) where it releases the oxygen to burn nutrients to provide energy to power the functions of the organism, and collects the resultant carbon dioxide to bring it back to the respiratory organs to be dispensed from the organism.
In mammals, the protein makes up about 97% of the red blood cells' dry content, and around 35% of the total content (including water).[citation needed] Hemoglobin has an oxygen binding capacity of 1.34 ml O2 per gram of hemoglobin, which increases the total blood oxygen capacity seventy-fold compared to dissolved oxygen in blood. The mammalian hemoglobin molecule can bind (carry) up to four oxygen molecules.
Hemoglobin is involved in the transport of other gases: it carries some of the body's respiratory carbon dioxide (about 10% of the total) as carbaminohemoglobin, in which CO2 is bound to the globin protein. The molecule also carries the important regulatory molecule nitric oxide bound to a globin protein thiol group, releasing it at the same time as oxygen.
Hemoglobin is also found outside red blood cells and their progenitor lines. Other cells that contain hemoglobin include the A9 dopaminergic neurons in the substantia nigra, macrophages, alveolar cells, and mesangial cells in the kidney. In these tissues, hemoglobin has a non-oxygen-carrying function as an antioxidant and a regulator of iron metabolism.
Hemoglobin and hemoglobin-like molecules are also found in many invertebrates, fungi, and plants. In these organisms, hemoglobins may carry oxygen, or they may act to transport and regulate other things such as carbon dioxide, nitric oxide, hydrogen sulfide and sulfide. A variant of the molecule, called leghemoglobin, is used to scavenge oxygen, to keep it from poisoning anaerobic systems, such as nitrogen-fixing nodules of leguminous plants.
This text uses material from Wikipedia and is available under the GNU Free Documentation License.
Researchers propose a novel prognostic model for disease-specific survival in BCa patients
A new study from Japan investigated various prognostic indicators, including clinico-pathological and pre-operative hematological factors to develop a novel prognostic factors-based risk stratification model for disease-specific ...
Cancer
Mar 18, 2013 |
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Cellular bells: Key step in manufacture of red blood cells decoded
A healthy adult must generate as many as one hundred billion new red blood cells each day, to maintain the numbers circulating in his blood. A team of EPFL researchers has identified a key step in the process by which red ...
Medical research
Mar 14, 2013 |
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Study identifies 75 genetic regions that influence red blood cell formation
New research is revealing how red blood cells are made and how the body regulates the amount of haemoglobin that is packaged in red blood cells at any time. Genomic analysis techniques have doubled the number of genetic regions ...
Genetics
Dec 05, 2012 |
4.7 / 5 (3) |
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Researchers make less carcinogenic cigarette
(Medical Xpress) -- Though emphasizing that quitting is the best remedy to combat health problems for smokers, Cornell researchers have found a way to make cigarettes less toxic.
Health
Jan 03, 2012 |
4 / 5 (4) |
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New screening method can detect a range of clinical conditions from a single dried blood spot
Scientists have developed a rapid method that can be used to simultaneously screen patients for a range of genetic and acquired clinical conditions from a single dried blood spot.
Diseases, Conditions, Syndromes
Nov 16, 2011 |
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