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  2. Hemoglobin - Wikipedia

    en.wikipedia.org/wiki/Hemoglobin

    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 ...

  3. Oxygen–hemoglobin dissociation curve - Wikipedia

    en.wikipedia.org/wiki/Oxygenhemoglobin...

    Hemoglobin (Hb) is the primary vehicle for transporting oxygen in the blood. Each hemoglobin molecule has the capacity to carry four oxygen molecules. These molecules of oxygen bind to the globin chain of the heme prosthetic group. [1] When hemoglobin has no bound oxygen, nor bound carbon dioxide, it has the unbound conformation (shape). The ...

  4. Bohr effect - Wikipedia

    en.wikipedia.org/wiki/Bohr_effect

    The Bohr effect increases the efficiency of oxygen transportation through the blood. After hemoglobin binds to oxygen in the lungs due to the high oxygen concentrations, the Bohr effect facilitates its release in the tissues, particularly those tissues in most need of oxygen. When a tissue's metabolic rate increases, so does its carbon dioxide ...

  5. Heme - Wikipedia

    en.wikipedia.org/wiki/Heme

    Binding of oxygen to a heme prosthetic group. Heme (American English), or haem (Commonwealth English, both pronounced /hi:m/ HEEM), is a ring-shaped iron-containing molecular component of hemoglobin, which is necessary to bind oxygen in the bloodstream. It is composed of four pyrrole rings with 2 vinyl and 2 propionic acid side chains. [1]

  6. Blood - Wikipedia

    en.wikipedia.org/wiki/Blood

    Hemoglobin has an oxygen binding capacity between 1.36 and 1.40 ml O 2 per gram hemoglobin, [23] which increases the total blood oxygen capacity seventyfold, [24] compared to if oxygen solely were carried by its solubility of 0.03 ml O 2 per liter blood per mm Hg partial pressure of oxygen (about 100 mm Hg in arteries).

  7. Hemoglobin A - Wikipedia

    en.wikipedia.org/wiki/Hemoglobin_A

    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 ]

  8. Fick principle - Wikipedia

    en.wikipedia.org/wiki/Fick_principle

    Measuring the content of hemoglobin in the blood and the percentage of saturation of hemoglobin (the oxygen saturation of the blood) is a simple process and is readily available to physicians. Using the fact that each gram of hemoglobin can carry 1.34 mL of O 2 , the oxygen content of the blood (either arterial or venous) can be estimated by ...

  9. Oxygen saturation (medicine) - Wikipedia

    en.wikipedia.org/wiki/Oxygen_saturation_(medicine)

    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 of glucose metabolism also found in stored blood products) are increased. When the hemoglobin ...

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