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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 ...
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 ...
It owes its color to hemoglobin, to which oxygen binds. Deoxygenated blood is darker due to the difference in shape of the red blood cell when oxygen binds to haemoglobin in the blood cell (oxygenated) versus does not bind to it (deoxygenated). Though veins might make it appear as such, human blood is never naturally blue. [3]
hemoglobin: HB: heart block: Hb% hemoglobin concentration in gram per deciliter HbA: hemoglobin A (commonest type of hemoglobin) HbA1c: glycated hemoglobin (used as a measure of diabetes control) HBD: has been drinking HbF: fetal hemoglobin: HBO: hyperbaric oxygen: HBP: high blood pressure, that is, hypertension: Hb s Ag: Hepatitis B surface ...
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 ...
Carbon monoxide, for example, is extremely dangerous when carried to the blood via the lungs by inhalation, because carbon monoxide irreversibly binds to hemoglobin to form carboxyhemoglobin, so that less hemoglobin is free to bind oxygen, and fewer oxygen molecules can be transported throughout the blood. This can cause suffocation insidiously.
The Haldane effect is a property of hemoglobin first described by John Scott Haldane, within which oxygenation of blood in the lungs displaces carbon dioxide from hemoglobin, increasing the removal of carbon dioxide. Consequently, oxygenated blood has a reduced affinity for carbon dioxide.
Hemoglobin A (HbA), also known as adult hemoglobin, hemoglobin A1 or α 2 β 2, is the most common human hemoglobin tetramer, accounting for over 97% of the total red blood cell hemoglobin. [1] Hemoglobin is an oxygen-binding protein, found in erythrocytes , which transports oxygen from the lungs to the tissues. [ 2 ]