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  2. Near-infrared window in biological tissue - Wikipedia

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

    These two different types of hemoglobin exhibit different absorption spectra that are normally represented in terms of molar extinction coefficients, as shown in Figure 1. The molar extinction coefficient of Hb has its highest absorption peak at 420 nm and a second peak at 580 nm. Its spectrum then gradually decreases as light wavelength increases.

  3. Molar absorption coefficient - Wikipedia

    en.wikipedia.org/wiki/Molar_absorption_coefficient

    c is the molar concentration of those species; ℓ is the path length. Different disciplines have different conventions as to whether absorbance is decadic (10-based) or Napierian (e-based), i.e., defined with respect to the transmission via common logarithm (log 10) or a natural logarithm (ln). The molar absorption coefficient is usually decadic.

  4. Isosbestic point - Wikipedia

    en.wikipedia.org/wiki/Isosbestic_point

    When an isosbestic plot is constructed by the superposition of the absorption spectra of two species (whether by using molar absorptivity for the representation, or by using absorbance and keeping the same molar concentration for both species), the isosbestic point corresponds to a wavelength at which these spectra cross each other.

  5. File:Fig 1 - The molar extinction coefficient of HbO2 and Hb.png

    en.wikipedia.org/wiki/File:Fig_1_-_The_molar...

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  6. Why the Amazon's biggest fish is quickly going extinct - AOL

    www.aol.com/news/2014-08-14-why-the-amazons...

    A massive species of fish that used to dominate the Amazon river is quickly dying out in several areas. A recent study of fishing communities in the state of Amazonas, Brazil found the giant ...

  7. Root effect - Wikipedia

    en.wikipedia.org/wiki/Root_Effect

    The Root effect is a physiological phenomenon that occurs in fish hemoglobin, named after its discoverer R. W. Root.It is the phenomenon where an increased proton or carbon dioxide concentration (lower pH) lowers hemoglobin's affinity and carrying capacity for oxygen.

  8. Hemocyanin - Wikipedia

    en.wikipedia.org/wiki/Hemocyanin

    Hemoglobin binds oxygen cooperatively due to steric conformation changes in the protein complex, which increases hemoglobin's affinity for oxygen when partially oxygenated. In some hemocyanins of horseshoe crabs and some other species of arthropods , cooperative binding is observed, with Hill coefficients of 1.6–3.0.

  9. Channichthyidae - Wikipedia

    en.wikipedia.org/wiki/Channichthyidae

    The hemoglobin protein is made of two subunits (alpha and beta). In 15 of the 16 icefish species, the beta subunit gene has been completely deleted and the alpha subunit gene has been partially deleted. [13] One icefish species, Neopagetopsis ionah, has a more complete hemoglobin beta subunit, but a still nonfunctional, hemoglobin gene. [14]