News tagged with hemoglobin
Twisting of protein molecules in water is successfully captured on molecular movie
A research group led by Hyotcherl Ihee at the Korea Advanced Institute of Science and Technology (KAIST) observed twisting of protein molecules in an aqueous solution (which is very similar to the environment ...
Apr 27, 2012 |
not rated yet |
0
Unique E. coli protein may be not after all
A bacterial protein recently thought to be a unique mechanism for utilizing iron may not be after all. Researchers from the University of Georgia, the Fellowship for Interpretation of Genomes, the University of Oklahoma and ...
Jan 03, 2012 |
2.5 / 5 (8) |
0
Woolly mammoth's secrets for shrugging off cold points toward new artificial blood for humans
The blood from woolly mammoths -- those extinct elephant-like creatures that roamed the Earth in pre-historic times -- is helping scientists develop new blood products for modern medical procedures that involve ...
Sep 14, 2011 |
4.8 / 5 (4) |
2
|
Ringing the hemoglobin bell
(PhysOrg.com) -- Knowing the structure of a molecule is an important part of understanding it, but quite often its even more important to know how the molecule moves -- more specifically, the vibrational ...
Sep 08, 2011 |
not rated yet |
0
|
Worm study yields insights on humans, parasites and iron deficiency
Using a tiny bloodless worm, University of Maryland Associate Professor Iqbal Hamza and his team have discovered a large piece in the puzzle of how humans, and other organisms safely move iron around in the ...
May 26, 2011 |
5 / 5 (1) |
0
|
Researchers develop technique for measuring stressed molecules in cells
Biophysicists at the University of Pennsylvania have helped develop a new technique for studying how proteins respond to physical stress and have applied it to better understand the stability-granting structures in normal ...
May 03, 2011 |
not rated yet |
0
|
Iowa State, Ames Lab researcher hunts for green catalysts
L. Keith Woo is searching for cleaner, greener chemical reactions. Woo, an Iowa State University professor of chemistry and an associate of the U.S. Department of Energy's Ames Laboratory, has studied catalysts ...
Mar 07, 2011 |
not rated yet |
0
Investigating sickle cell disease
Until recently, the pairing of molecular biology and mechanical engineering would have been viewed as highly unusual. But thanks to an explosion of imaging and simulation techniques over the past few decades, ...
Medicine & Health / Diseases, Conditions, Syndromes
Feb 25, 2011 |
5 / 5 (1) |
0
Direct observation of carbon monoxide binding to metal-porphyrines
What makes carbon monoxide so toxic is that it blocks the binding site for oxygen in hemoglobin. This very mechanism, if better understood, could be used to implement sensors to warn against carbon monoxide. ...
Jan 10, 2011 |
not rated yet |
0
|
Poor response to anti-anemia drug predicts higher risk of heart disease or death
Patients with diabetes, kidney disease and anemia who don't respond to treatment with an anti-anemia drug have a higher risk of cardiovascular disease or death, researchers at UT Southwestern Medical Center have found.
Medicine & Health / Diseases, Conditions, Syndromes
Dec 29, 2010 |
3.5 / 5 (2) |
1
Increasing oxygen delivery: Allosteric effectors of human hemoglobin
(PhysOrg.com) -- Numerous diseases, such as cardiovascular ailments and cancer, are characterized by a lack of oxygen in specific tissues. Therefore, increasing the supply of oxygen delivered by red blood ...
Dec 23, 2010 |
4.5 / 5 (2) |
2
Don't trouble your heart: Naturally high hemoglobin OK in dialysis patients
Naturally occurring high hemoglobin levels are safe for kidney disease patients on dialysis, according to a study appearing in an upcoming issue of the Journal of the American Society Nephrology (JASN). The results sugge ...
Medicine & Health / Diseases, Conditions, Syndromes
Dec 16, 2010 |
not rated yet |
1
Hemodynamic responses to the mother's face in infants by near-infrared spectroscopy
A Japanese research group led by Prof. Ryusuke Kakigi and Dr. Emi Nakato (National Institute for Physiological Sciences: NIPS) and Prof. Masami K Yamaguchi (Chuo University) found that there was the different hemodynamic ...
Medicine & Health / Neuroscience
Dec 16, 2010 |
not rated yet |
0
Blood-sucking superbug prefers taste of humans
"Staph" bacteria feed on blood. They need the iron that's hidden away inside red blood cells to grow and cause infections. It turns out that these microbial vampires prefer the taste of human blood, Vanderbilt ...
Dec 15, 2010 |
not rated yet |
0
Alternating stacks of planar cations and dipyrrole-containing anions provides concept for new materials
(PhysOrg.com) -- Pyrroles, which are rings containing one nitrogen and four carbon atoms, are essential components of our red hemoglobin as well as the green chlorophyll in plants. Japanese researchers led ...
Dec 10, 2010 |
5 / 5 (3) |
0
|
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.
For more information about Hemoglobin, read the full article at
Wikipedia.
This text uses material from Wikipedia and is available under the GNU Free Documentation License.