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  2. Oxygen–hemoglobin dissociation curve - Wikipedia

    en.wikipedia.org/wiki/Oxygen–hemoglobin...

    This curve is an important tool for understanding how our blood carries and releases oxygen. Specifically, the oxyhemoglobin dissociation curve relates oxygen saturation (SO 2) and partial pressure of oxygen in the blood (PO 2), and is determined by what is called "hemoglobin affinity for oxygen"; that is, how readily hemoglobin acquires and ...

  3. Blood-oxygenation-level–dependent imaging - Wikipedia

    en.wikipedia.org/wiki/Blood-oxygenation-level...

    Through a process called the haemodynamic response, blood releases oxygen to active neurons at a greater rate than to inactive neurons. This causes a change of the relative levels of oxyhemoglobin and deoxyhemoglobin (oxygenated or deoxygenated blood) that can be detected on the basis of their differential magnetic susceptibility.

  4. Near-infrared window in biological tissue - Wikipedia

    en.wikipedia.org/wiki/Near-infrared_window_in...

    In addition to the total concentration of hemoglobin, the oxygen saturation will define the concentration of oxy- and deoxyhemoglobin in tissue and so the total absorption spectrum. Depending on the type of tissue, we can consider different situations. Below, the total concentration of hemoglobin is assumed to be 2.3 mM.

  5. CO-oximeter - Wikipedia

    en.wikipedia.org/wiki/CO-oximeter

    Finger tip carboxyhemoglobin saturation monitor.. A CO-oximeter is a device that measures the oxygen carrying state of hemoglobin in a blood specimen, including oxygen-carrying hemoglobin (O2Hb), non-oxygen-carrying but normal hemoglobin (HHb) (formerly, but incorrectly, referred to as 'reduced' hemoglobin), as well as the dyshemoglobins such as carboxyhemoglobin (COHb) and methemoglobin (MetHb).

  6. 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]

  7. Haldane effect - Wikipedia

    en.wikipedia.org/wiki/Haldane_effect

    In the oxygen-rich capillaries of the lung, this property causes the displacement of carbon dioxide to plasma as low-oxygen blood enters the alveolus and is vital for alveolar gas exchange. The general equation for the Haldane Effect is: H + + HbO 2 ⇌ H + Hb + O 2; However, this equation is confusing as it reflects primarily the Bohr effect.

  8. Globin - Wikipedia

    en.wikipedia.org/wiki/Globin

    They bind oxygen, and act to initiate an aerotactic response or regulate gene expression. [16] [17] Protoglobin: a single domain globin found in archaea that is related to the N-terminal domain of globin-coupled sensors. [18] Truncated 2/2 globin: lack the first helix, giving them a 2-over-2 instead of the canonical 3-over-3 alpha-helical ...

  9. Root effect - Wikipedia

    en.wikipedia.org/wiki/Root_Effect

    This results in the Hb-O 2 dissociation curve being shifted downward and not just to the right. At low pH, hemoglobins showing the Root effect don't become fully oxygenated even at oxygen tensions up to 20kPa. [2] This effect allows hemoglobin in fish with swim bladders to unload oxygen into the swim bladder against a high oxygen gradient. [3]

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