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  2. Hemoglobin - Wikipedia

    en.wikipedia.org/wiki/Hemoglobin

    The Bohr effect favors the T state rather than the R state. (shifts the O 2-saturation curve to the right). Conversely, when the carbon dioxide levels in the blood decrease (i.e., in the lung capillaries), carbon dioxide and protons are released from hemoglobin, increasing the oxygen affinity of the protein.

  3. Oxygen–hemoglobin dissociation curve - Wikipedia

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

    The T state has a lower affinity for oxygen than the R state, so with increased acidity, the hemoglobin binds less O 2 for a given P O2 (and more H +). This is known as the Bohr effect . [ 4 ] A reduction in the total binding capacity of hemoglobin to oxygen (i.e. shifting the curve down, not just to the right) due to reduced pH is called the ...

  4. Bohr effect - Wikipedia

    en.wikipedia.org/wiki/Bohr_effect

    In the R state, the ionic pairings are absent, meaning that the R state's stability increases when the pH increases, as these residues are less likely to stay protonated in a more basic environment. The Bohr effect works by simultaneously destabilizing the high-affinity R state and stabilizing the low-affinity T state, which leads to an overall ...

  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. Carbaminohemoglobin - Wikipedia

    en.wikipedia.org/wiki/Carbaminohemoglobin

    When carbon dioxide binds to hemoglobin, carbaminohemoglobin is formed, lowering hemoglobin's affinity for oxygen via the Bohr effect. The reaction is formed between a carbon dioxide molecule and an amino residue. [12] In the absence of oxygen, unbound hemoglobin molecules have a greater chance of becoming carbaminohemoglobin.

  7. Near-infrared window in biological tissue - Wikipedia

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

    The near-infrared (NIR) window (also known as optical window or therapeutic window) defines the range of wavelengths from 650 to 1350 nanometre (nm) where light has its maximum depth of penetration in tissue. [1] Within the NIR window, scattering is the most dominant light-tissue interaction, and therefore the propagating light becomes diffused ...

  8. Travel Worry-Free with These Innovative Automatic Pet Feeders

    www.aol.com/travel-worry-free-innovative...

    With a capacity of 50 pounds of grain or pellets and 25 pounds of dog/cat food, this feeder is designed with larger pets (think horses) in mind, though the Quick Feeder is versatile, with portions ...

  9. Root effect - Wikipedia

    en.wikipedia.org/wiki/Root_Effect

    It is the phenomenon where an increased proton or carbon dioxide concentration (lower pH) lowers hemoglobin's affinity and carrying capacity for oxygen. [1] [2] The Root effect is to be distinguished from the Bohr effect where only the affinity to oxygen is reduced. Hemoglobins showing the Root effect show a loss of cooperativity at low pH.