Search results
Results from the WOW.Com Content Network
The oxygen–hemoglobin dissociation curve, also called the oxyhemoglobin dissociation curve or oxygen dissociation curve (ODC), is a curve that plots the proportion of hemoglobin in its saturated (oxygen-laden) form on the vertical axis against the prevailing oxygen tension on the horizontal axis. This curve is an important tool for ...
Hemoglobin in the blood carries oxygen from the respiratory organs (lungs or gills) to the other tissues of the body, where it releases the oxygen to enable aerobic respiration which powers an animal's metabolism. A healthy human has 12 to 20 grams of hemoglobin in every 100 mL of blood. Hemoglobin is a metalloprotein, a chromoprotein, and ...
A CO-oximeter measures the absorption of light passing through blood from few as two or three wavelengths of light to several dozens of wavelengths, in order to distinguish oxyhemoglobin, and deoxyhemoglobin (formerly called 'reduced' hemoglobin), and thus determine the oxyhemoglobin saturation (the percentage of oxygenated hemoglobin compared to the total amount of available hemoglobin (Hb)).
Carboxyhemoglobin (carboxyhaemoglobin BrE) (symbol COHb or HbCO) is a stable complex of carbon monoxide and hemoglobin (Hb) that forms in red blood cells upon contact with carbon monoxide. Carboxyhemoglobin is often mistaken for the compound formed by the combination of carbon dioxide and hemoglobin, which is actually carbaminohemoglobin.
Hemoglobin, for comparison, has a Hill coefficient of usually 2.8–3.0. In these cases of cooperative binding hemocyanin was arranged in protein sub-complexes of 6 subunits (hexamer) each with one oxygen binding site; binding of oxygen on one unit in the complex would increase the affinity of the neighboring units.
Hemoglobin's oxygen binding affinity (see oxygen–haemoglobin dissociation curve) is inversely related both to acidity and to the concentration of carbon dioxide. [1] That is, the Bohr effect refers to the shift in the oxygen dissociation curve caused by changes in the concentration of carbon dioxide or the pH of the environment.
The affinity of hemoglobin to oxygen may impair or enhance oxygen release at the tissue level. Oxygen is more readily released to the tissues (i.e., hemoglobin has a lower affinity for oxygen) when pH is decreased, body temperature is increased, arterial partial pressure of carbon dioxide (PaCO 2 ) is increased, and 2,3-DPG levels (a byproduct ...
Hemoglobin F, like adult hemoglobin (hemoglobin A and hemoglobin A2), has four subunits or chains. Each subunit contains a heme group with an iron element which is key in allowing the binding and unbinding of oxygen. As such, hemoglobin F can adopt two states: oxyhemoglobin (bound to oxygen) and deoxyhemoglobin (without oxygen).