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  • Hemoglobin


    Hemoglobin (American) or haemoglobin (British) (); abbreviated Hb or Hgb, is the iron-containing oxygen-transport metalloprotein in the red blood cells (erythrocytes) of almost all vertebrates (the exception being the fish family Channichthyidae) as well as the tissues of some invertebrates. Haemoglobin in the blood carries oxygen from the lungs or gills to the rest of the body (i.e. the tissues). There it releases the oxygen to permit aerobic respiration to provide energy to power the functions of the organism in the process called metabolism. A healthy individual has 12 to 16 grams of haemoglobin in every 100 ml of blood. In mammals, the protein makes up about 96% of the red blood cells' dry content (by weight), and around 35% of the total content (including water). Haemoglobin has an oxygen-binding capacity of 1.34 mL O2 per gram, which increases the total blood oxygen capacity seventy-fold compared to dissolved oxygen in blood. The mammalian hemoglobin molecule can bind (carry) up to four oxygen molecules. Hemoglobin is involved in the transport of other gases: It carries some of the body's respiratory carbon dioxide (about 20–25% of the total) as carbaminohemoglobin, in which CO2 is bound to the heme protein. The molecule also carries the important regulatory molecule nitric oxide bound to a globin protein thiol group, releasing it at the same time as oxygen. Haemoglobin is also found outside red blood cells and their progenitor lines. Other cells that contain haemoglobin include the A9 dopaminergic neurons in the substantia nigra, macrophages, alveolar cells, lungs, retinal pigment epithelium, hepatocytes, mesangial cells in the kidney, endometrial cells, cervical cells and vaginal epithelial cells. In these tissues, haemoglobin has a non-oxygen-carrying function as an antioxidant and a regulator of iron metabolism. Haemoglobin and haemoglobin-like molecules are also found in many invertebrates, fungi, and plants. In these organisms, haemoglobins may carry oxygen, or they may act to transport and regulate other small molecules and ions such as carbon dioxide, nitric oxide, hydrogen sulfide and sulfide. A variant of the molecule, called leghaemoglobin, is used to scavenge oxygen away from anaerobic systems, such as the nitrogen-fixing nodules of leguminous plants, before the oxygen can poison (deactivate) the system.

  • Oxygen saturation (medicine)


    Blood circulation: Red = oxygenated (arteries), Blue = deoxygenated (veins)Oxygen saturation is the fraction of oxygen-saturated hemoglobin relative to total hemoglobin (unsaturated + saturated) in the blood. The human body requires and regulates a very precise and specific balance of oxygen in the blood. Normal blood oxygen levels in humans are considered 95–100 percent. If the level is below 90 percent, it is considered low resulting in hypoxemia. Blood oxygen levels below 80 percent may compromise organ function, such as the brain and heart, and should be promptly addressed. Continued low oxygen levels may lead to respiratory or cardiac arrest. Oxygen therapy may be used to assist in raising blood oxygen levels. Oxygenation occurs when oxygen molecules () enter the tissues of the body. For example, blood is oxygenated in the lungs, where oxygen molecules travel from the air and into the blood. Oxygenation is commonly used to refer to medical oxygen saturation.

  • Hemoglobinemia


    Hemoglobinemia (British Haemoglobinaemia) is a medical condition in which there is an excess of hemoglobin in the blood plasma, sometimes abbreviated as Hb. This is an effect of intravascular hemolysis, in which hemoglobin separates from red blood cells, a form of anemia. Hemoglobinemia can be caused by intrinisic or extrinsic factors. When hemoglobinemia is internally caused, it is a result of recessive genetic defects that cause the red blood cells to lyse, letting the hemoglobin spill out of the cell into the blood plasma. In intravascular hemolysis, hemoglobin is released and binds with haptoglobin. This causes haptoglobin levels to decrease; once haptoglobin is saturated, excess hemoglobin is filtered in the kidney and reabsorbed in the proximal tubules. In externally caused hemoglobinemia, an outside attacker acts as an antibody against the red blood cells. This can cause the cells to be destroyed and their hemoglobin released. In extravascular hemolysis, red blood cells are phagocytized by macrophages in the spleen and liver.

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