As I understand it, and very simplistically, I think it means that the bonding is easily reversible. In other words, the O2 is readily bound to haemoglobin but is also readily released depending on the partial saturation levels of Oxygen (PO2) that are encountered by the RBC. * In the pulmonary capillaries the PO2 is high and therefore the amount of O2 bound to Hb is also high (fully saturated). In the systemic capillaries the PO2 is low and hence the O2 dissociates with the Hb and diffuses into the tissue cells. (The Hb is then said to be partially saturated). Although PO2 is the major factor in the binding of O2 to Hb, other factors also effect this process. * Acidity: Lactic acid and carbonic acid generated during exercise lowers the pH of the blood which promotes the release of O2 from Hb. Hence the exercising tissues which require extra O2 help create a situation where more O2 is available. * PCO2 effects the transport and delivery of O2. Increased metabolic activity of the tissue cells produces more CO2 as waste, which promotes release of O2 from Hb through an associated decrease in pH (see above point) and also as part of an O2/CO2 cycle. It goes something like this:
In the pulmonary capillaries, O2 diffuses from the alveolus into the RBC. It binds to Hb to create oxyhaemoglobin and H+ ions. Bicarbonate ions combine with the H+ ions to create carbonic acid which, under the influence of the enzyme carbonic anhydrase, dissociates into CO2 and water. The CO2 diffuses into the alveoli and is expelled by the lungs.
The RBC then travels in the blood to the systemic capillaries and CO2 diffuses from the tissues (as a waste product of tissue cell metabolism) into the RBC. A small percentage of the CO2 binds to the globin in Hb, forming carbaminohaemoglobin, this causes O2 to dissociate from the haem part of the Hb. The O2 then diffuses from the RBC into the tissue cells.
Most of the CO2, under the influence of the enzyme carbonic anhydrase, combines with H2O to become Carbonic acid which then dissociates into Bicarbonate ions (HCO3-) and H+ ions. The H+ ions promote the dissociation of O2 from the haemoglobin by taking the place of the O2 in the Hb molecule. * Increased temperature also has a minor effect of promoting the release of O2 from the Hb. Anatomy and physiology books such as "Anatomy and Physiology - From Science to Life" by Jenkins Kemnitz and Tortora is a fabulous resource for understanding the intricacies of this process.
Hemoglobin has a high affinity for oxygen, allowing it to bind oxygen molecules in the lungs where oxygen concentration is high. This binding is reversible, meaning that hemoglobin can release oxygen molecules in tissues where oxygen concentration is lower. This enables efficient delivery of oxygen throughout the body.
Carbon monoxide in cigarette smoke is the main chemical that causes a lack of oxygen in the body. It binds to hemoglobin in the blood more readily than oxygen, reducing the amount of oxygen that can be transported around the body. This can lead to a decrease in oxygen levels in the blood and tissues, contributing to the harmful effects of smoking on health.
It is said to be anaerobic, which means "without oxygen". The opposite of "anaerobic" is "aerobic" which means requiring oxygen.
Oxidation means addition of oxygen. When oxygen is added to a compound, it is said to be oxidised.
Reactive.
There is a very small amount of oxygen on Mars. The oxygen level in Marsâ?? atmosphere said to be around .145%.
Oxygen is transported first by air down the trachea and then transform to the hemoglobin of the blood to the cells. This is the pathway of oxygen in the human system.
Yes, of course! Low Hemoglobin means anemia, and it is said that "there are not leukemia without anemia"
Water, H2O, is a molecule of hydrogen and oxygen. It is considered a compound. That said, yes, oxygen and hydrogen combine to make a compound that is represented by the molecule H2O.
Do hemoglogin electrophoresis
It has this four part structure because it can carry 4 irons. That makes it capable of carry as much oxygen as it possibly can. When this structure was first described, others said that it is way too big to work and would not fit in red blood cells. But it does work and the body gets the oxygen it needs.
John Dalton
Carbon monoxide in cigarette smoke is the main chemical that causes a lack of oxygen in the body. It binds to hemoglobin in the blood more readily than oxygen, reducing the amount of oxygen that can be transported around the body. This can lead to a decrease in oxygen levels in the blood and tissues, contributing to the harmful effects of smoking on health.
It is said to be anaerobic, which means "without oxygen". The opposite of "anaerobic" is "aerobic" which means requiring oxygen.
Hemoglobin is a very large molecule that has iron in its' structure. The iron carries oxygen. There were many people involved in the work to uncover it. In 1825 J.F. Engelhard said that a very large protein carried iron. Adair confirmed Engelhard's results in 1925. Hemoglobin itself was discovered by Hünefeld in 1840. In 1851 German physiologist Otto Funke added more data. In 1959 Max Perutz determined the molecular structure of myoglobin (similar to hemoglobin) and he shared the 1962 Nobel Prize in Chemistry.
Oxidation means addition of oxygen. When oxygen is added to a compound, it is said to be oxidised.
Elements form together to create compounds such as H2O-water it is just two hydrogen and one oxygen. This is also known as dihydrogenmonoxide (said- di...hydrogen...mon..oxide), without this coumpound there would be no living oranisms
Reactive.