explain......the oxygen capacity of hemoglobin?
825942
Short and sweet\n\n1.) Each Hemoglobin can carry four oxygen molecules\n\n2.) The binding of one oxygen molecule to hemoglobin induces a conformational change to make it easier for the next oxygen molecule to bind, which makes it easier for the third, which makes it easier for the fourth.\n\n3.) Similarly, with a full hemoglobin, after the first oxygen is released, it's easier for the second one to come off and so on. This phenomenon is why all the oxygen isn't released into the tissue right after it leaves the heart.\n\n4.) Look both ways when crossing the street.
179057
It's not C.  An increase in pH makes a solution more alkaline, meaning less H+ in the fluids.\n\nI'm going to say A here because a rise in pH is associated with increased O2 binding to hemoglobin.
439771
There are two oxygen carrying mechanisms in the blood. One is dissolved oxygen in the plasma. The other is hemoglobin, the red colored stuff in the red blood cells. It combines with oxygen in the lungs, and releases it in the tissues, where it picks up CO2. CO2 also dissolves in the plasma, and both tend to give it up in the lungs. \n\nSaturation is a measure of how much oxygen is in the blood sampled as compared to the maximum possible. In hospitals, it is non-invasively measured by optical sensing through a finger tip. It's that little glowing clamp thing they stick on a finger. \n\nThis works because oxygen carrying hemoglobin is 'redder' than non-oxygen carrying hemoglobin. But it doesn't include the oxygen carried by the plasma, since plasma with oxygen isn't noticeably different in color than plasma with less oxygen in it. So this measurement isn't (quite) accurate since it's not really measuring all the oxygen present. \n\nBut this is clinically useful because it's a reasonable measure of what's really the point of bothering with oxygen saturation at all. some lung conditions interfere with the transfer of oxygen and CO2 in the lungs. Since the hemoglobin saturation participates in that transfer, how well it's been saturated can be used for practical clinical indications. We don't really need to know exactly what the oxygen saturation is, since, if it's good enough, that's all we need to know. Only if there's some major problem, will we need to know anything more detailed.
572827
Its like gas for a car. Blood is a oxygen carrier, and supports all the body organs. If anyone loses too much of it- too bad!
541170
New in Chemistry?????\n\nThere is no conversion of H2O in HHO.\nIt is simply way of writing a formula. HHO is wrong, it is HOH.\n\nActually Oxygen has two separate bonds with two different atoms of Hydrogen so it is written as H-O-H.\n\nWhen H-O-H is broken it usually converts to H+ and OH-
392229
At the alveoli; the capillary bed is dense and near the surface there, so oxygen binds to hemoglobin there.
951552
Haemoglobin is a kind of cell that you have in your blood that carries oxygen. Glucose sticks to the out side of the cells, which last about 6 weeks. The HbA1c test tests how much glucose is stuck to your haemoglobin and this gives you an indication of how much has stuck in the last 6 weeks, which gives a rough idea of how your diabetes control has been. The results sound pretty similar to your blood glucose results (eg. 7.2) but they should not be confused - a HbA1c of 7.2 does not mean that this is your average blood sugar. It's used to find out how your overall control has been recently because even if you do several blood tests a day it wont tell you how your control is between times.
281418
Well, Every single cell in the body needs oxygen. If hemoglobin is malformed because of a mutation, there will be no cells in the body that can function properly due to the lack of adequate amounts of oxygen being transported to the cells. Since all body systems rely on the cell for functionality, no body system will go unaffected.
432294
Each hemoglobin molecule has 4 heme groups. Each heme group binds to one oxygen molecule. This happens in the lung. The hemoglobin is 98-100% saturated. In the tissues, in normal conditions, the saturation is reduced to 75%. So not all the oxgen molecules are given up. Only 25%.
598955
not drowning and suffocating...you will feel drowsy and come to a never ending sleep...\n\nCO, binds to the haemogloin in blood which is responsible for carry oxygen throughout the body...\n\nCO has higher affinity to Haemoglobin than O2, so it binds faster and blocks the binding of O2. its like someones smothering you but u cant feel it.
579619
Oxygen bind to hemoglobin which is part of the red blood cells.  It is picked up in the lungs where there are little sacs that have a very thin lining of cells.  Therefore the air you breathe in will be able to reach the blood.  Then the hemoglobin will carry blood to the parts of the body.
825900
Both mother and fetus share a common blood supply. In particular, the fetus's blood supply is delivered via the umbilical vein from the placenta, which is anchored to the wall of the mother's uterus. As blood courses through the mother, oxygen is delivered to capillary beds for gas exchange, and by the time blood reaches the capillaries of the placenta, its oxygen saturation has decreased considerably. In order to recover enough oxygen to sustain itself, the fetus must be able to bind oxygen with a greater affinity than the mother.\n\nFetal hemoglobin's affinity for oxygen is substantially greater than that of adult hemoglobin. Notably, the P50 value for fetal hemoglobin (i.e., the partial pressure of oxygen at which the protein is 50% saturated; lower values indicate greater affinity) is roughly 19 mmHg, whereas adult hemoglobin has a value of approximately 26.8 mmHg. As a result, the so-called "oxygen saturation curve", which plots percent saturation vs. pO2, is left-shifted for fetal hemoglobin in comparison to the same curve in adult hemoglobin.\n\nThis greater affininty for oxygen is explained by fetal hemoglobin's interaction with 2,3-bisphosphoglycerate (2,3-BPG). In adult red blood cells, this substance decreases the affinity of hemoglobin for oxygen. It is also present in fetal red blood cells, but does not interact with fetal hemoglobin, leaving its affinity for oxygen unchanged. Adult hemoglobin alone actually has a higher affinity for oxygen than its fetal equivalent, but the levels of 2,3-BPG reduce it.
124983
The decreased hemaglobin synthesis in anemia is correct. What the others described may occur but is not the main mechanism. The decreased hemaglobin leads to a perfusion (oxygen delivery) problem. The lungs have a compensatory mechanism to match ventilation and perfusion. (This means that if a region of the lung has a decreased blood supply, the lungs bronchoconstrict to avoid wasting breathed in air.)\nWell, with severe anemia the perfusion problem is not regional but system wide, so there can a massive response of bronchoconstriction (think of the worst asmtha attack ever). This makes the situation worse obviously, less air reaches the alvoli for gas exchange, and you have acute respiratory failure. This response can occur when the body increases its oxygen demands for one reason or another(exercise, or illness come to mind).
264480
Oxygen enters the blood in the lungs, where is binds to hemoglobin (which has a strong oxygen-binding affinity). Hemoglobin travels through the blood until it reaches the blood vessels. Once blood reaches the muscles, the carbon dioxide produced by the muscles enters the blood in the form of carbonic acid. The carbonic acid lowers the blood pH, which lowers the affinity of hemoglobin to bind oxygen, releasing large amounts of oxygen into the working tissues of the muscle.
799721
A typical human erythrocyte (red blood cell) contains about 270 million haemoglobin molecules, with each carrying four heme groups.\n\nDecrease of hemoglobin, with or without an absolute decrease of red blood cells, leads to symptoms of anemia. Anemia has many different causes, although iron deficiency and its resultant iron deficiency anemia are the most common causes in the Western world. As absence of iron decreases heme synthesis, red blood cells in iron deficiency anemia are hypochromic (lacking the red hemoglobin pigment) and microcytic (smaller than normal).
118751
its where the blood picks up the oxygen.
1035133
By measuring the Biological Oxygen demand (BOD) or the Chemical oxygen demand (COD) \n\nhttp://en.wikipedia.org/wiki/Chemical_oxygen_demand\n\nhttp://en.wikipedia.org/wiki/BOD\n\nhope these are helpful :)