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

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

    Other methods which propose to measure neural activity directly have been attempted (for example, measurement of the Oxygen Extraction Fraction, or OEF, in regions of the brain, which measures how much of the oxyhemoglobin in the blood has been converted to deoxyhemoglobin [4]), but because the electromagnetic fields created by an active or ...

  3. Oxygen–hemoglobin dissociation curve - Wikipedia

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

    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 releases oxygen molecules into the fluid that surrounds it. Structure of oxyhemoglobin

  4. Haldane effect - Wikipedia

    en.wikipedia.org/wiki/Haldane_effect

    Histidine residues in hemoglobin can accept protons and act as buffers.Deoxygenated hemoglobin is a better proton acceptor than the oxygenated form. [1]In red blood cells, the enzyme carbonic anhydrase catalyzes the conversion of dissolved carbon dioxide to carbonic acid, which rapidly dissociates to bicarbonate and a free proton:

  5. Haemodynamic response - Wikipedia

    en.wikipedia.org/wiki/Haemodynamic_response

    The onset of neural activity leads to a systematic series of physiological changes in the local network of blood vessels that include changes in the cerebral blood volume per unit of brain tissue (CBV), changes in the rate of cerebral blood flow, and changes in the concentration of oxyhemoglobin and deoxyhemoglobin.

  6. Bohr effect - Wikipedia

    en.wikipedia.org/wiki/Bohr_effect

    Haemoglobin's affinity for CO is about 210 times stronger than its affinity for O 2, [14] meaning that it is very unlikely to dissociate, and once bound, it blocks the binding of O 2 to that subunit. At the same time, CO is structurally similar enough to O 2 to cause carboxyhemoglobin to favor the R state, raising the oxygen affinity of the ...

  7. 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).

  8. Venous blood - Wikipedia

    en.wikipedia.org/wiki/Venous_blood

    The color of human blood ranges from bright red when oxygenated to a darker red when deoxygenated. [2] 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).

  9. Arterial blood gas test - Wikipedia

    en.wikipedia.org/wiki/Arterial_blood_gas_test

    A low PaO 2 indicates abnormal oxygenation of blood and a person is known as having hypoxemia. (Note that a low PaO 2 is not required for the person to have hypoxia as in cases of Ischemia, a lack of oxygen in tissues or organs as opposed to arterial blood.) At a P a O 2 of less than 60 mm Hg, supplemental oxygen should be administered.