Carbaminohemoglobin: Difference between revisions
Undid revision 916208557 by 2405:204:858A:9253:0:0:1254:60AD (talk) reverting link-breaking edit |
I have deleted this sentence as no evidence is provided that carbaminohemoglobin is a blue colour. I am a Professsor in the hemoglobin field and have never heard of the idea, nor have some of my peers I discussed it with who have actually made measurements of CO2 bound to hemoglobin. I am of course happy to discuss the idea with the poster if he/she gives a reference to where they got this idea from. |
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== Mechanism == |
== Mechanism == |
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When carbon dioxide binds to hemoglobin, carbaminohaemoglobin is formed, lowering hemoglobin's affinity for [[oxygen]] via the [[Bohr effect]]. In the absence of oxygen, unbound hemoglobin molecules have a greater chance of becoming carbaminohaemoglobin. The [[Haldane effect]] relates to the increased affinity of de-oxygenated hemoglobin for [[Hydron (chemistry)|{{chem|H|+}}]]: offloading of oxygen to the tissues thus results in increased affinity of the hemoglobin for [[carbon dioxide]], and {{chem|H|+}}, which the body wants to get rid of, which can then be transported to the lung for removal. |
When carbon dioxide binds to hemoglobin, carbaminohaemoglobin is formed, lowering hemoglobin's affinity for [[oxygen]] via the [[Bohr effect]]. In the absence of oxygen, unbound hemoglobin molecules have a greater chance of becoming carbaminohaemoglobin. The [[Haldane effect]] relates to the increased affinity of de-oxygenated hemoglobin for [[Hydron (chemistry)|{{chem|H|+}}]]: offloading of oxygen to the tissues thus results in increased affinity of the hemoglobin for [[carbon dioxide]], and {{chem|H|+}}, which the body wants to get rid of, which can then be transported to the lung for removal. |
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Hemoglobin can bind to four molecules of carbon dioxide. The carbon dioxide molecules form a [[carbamate]] with the four terminal-amine groups of the four protein chains in the deoxy form of the molecule. Thus, one hemoglobin molecule can transport four carbon dioxide molecules back to the lungs, where they are released when the molecule changes back to the oxyhemoglobin form. |
Hemoglobin can bind to four molecules of carbon dioxide. The carbon dioxide molecules form a [[carbamate]] with the four terminal-amine groups of the four protein chains in the deoxy form of the molecule. Thus, one hemoglobin molecule can transport four carbon dioxide molecules back to the lungs, where they are released when the molecule changes back to the oxyhemoglobin form. |
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Revision as of 15:51, 28 October 2019
Carbaminohaemoglobin (or carbaminohaemoglobin, also known as carbhaemoglobin and carbohaemoglobin) is a compound of hemoglobin and carbon dioxide, and is one of the forms in which carbon dioxide exists in the blood. Twenty-three percent of carbon dioxide is carried in blood this way (70% is converted into bicarbonate by carbonic anhydrase and then carried in plasma, 7% carried as free CO2, in solution, or plasma).[1]
Mechanism
When carbon dioxide binds to hemoglobin, carbaminohaemoglobin is formed, lowering hemoglobin's affinity for oxygen via the Bohr effect. In the absence of oxygen, unbound hemoglobin molecules have a greater chance of becoming carbaminohaemoglobin. The Haldane effect relates to the increased affinity of de-oxygenated hemoglobin for H+
: offloading of oxygen to the tissues thus results in increased affinity of the hemoglobin for carbon dioxide, and H+
, which the body wants to get rid of, which can then be transported to the lung for removal.
Hemoglobin can bind to four molecules of carbon dioxide. The carbon dioxide molecules form a carbamate with the four terminal-amine groups of the four protein chains in the deoxy form of the molecule. Thus, one hemoglobin molecule can transport four carbon dioxide molecules back to the lungs, where they are released when the molecule changes back to the oxyhemoglobin form.
See also
References
- ^ Gas Transport in the Blood FIG. 18.11 Carbon dioxide transport
- Fogiel, M. (2004). Biology Problem Solver. Piscataway, New Jersey: Research & Education Association. p. 431. ISBN 0878915141.
External links
- carbaminohaemoglobin+A at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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