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  2. Bohr effect - Wikipedia

    en.wikipedia.org/wiki/Bohr_effect

    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.

  3. Hemoglobin - Wikipedia

    en.wikipedia.org/wiki/Hemoglobin

    In mammals, hemoglobin makes up about 96% of a red blood cell's dry weight (excluding water), and around 35% of the total weight (including water). [5] Hemoglobin has an oxygen-binding capacity of 1.34 mL of O 2 per gram, [6] which increases the total blood oxygen capacity seventy-fold compared to dissolved oxygen in blood plasma alone. [7]

  4. Oxygen–hemoglobin dissociation curve - Wikipedia

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

    Hemoglobin releases the bound oxygen when carbonic acid is present, as it is in the tissues. In the capillaries, where carbon dioxide is produced, oxygen bound to the hemoglobin is released into the blood's plasma and absorbed into the tissues. How much of that capacity is filled by oxygen at any time is called the oxygen saturation. Expressed ...

  5. 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). [24]

  6. Respiratory pigment - Wikipedia

    en.wikipedia.org/wiki/Respiratory_pigment

    Vertebrates use a tetrameric hemoglobin, carried in red blood cells, to breathe. There are multiple types of hemoglobin that have been found in the human body alone. Hemoglobin A is the “normal” hemoglobin, the variant of hemoglobin that is most common after birth. Hemoglobin A2 is a minor component of hemoglobin found in red blood cells.

  7. Hemodynamics - Wikipedia

    en.wikipedia.org/wiki/Hemodynamics

    Typical values for the viscosity of normal human plasma at 37 °C is 1.4 mN·s/m 2. [3] The viscosity of normal plasma varies with temperature in the same way as does that of its solvent water [4];a 3°C change in temperature in the physiological range (36.5°C to 39.5°C)reduces plasma viscosity by about 10%. [5]

  8. Red blood cell - Wikipedia

    en.wikipedia.org/wiki/Red_blood_cell

    As oxygen is released in the tissues, more CO 2 binds to hemoglobin, and as oxygen binds in the lung, it displaces the hemoglobin bound CO 2, this is called the Haldane effect. Despite the fact that only a small amount of the CO 2 in blood is bound to hemoglobin in venous blood, a greater proportion of the change in CO 2 content between venous ...

  9. Oxygen saturation (medicine) - Wikipedia

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

    Normal arterial blood oxygen saturation levels in humans are 96–100 percent. [1] If the level is below 90 percent, it is considered low and called hypoxemia . [ 2 ] Arterial blood oxygen levels below 80 percent may compromise organ function, such as the brain and heart, and should be promptly addressed.