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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.
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.
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.
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The magnitude of the constant φ may be higher than the value of the molar extinction coefficient, ε, for a species. When this is so, the detection limit for that species will be lower. At high solute concentrations, fluorescence intensity becomes non-linear with respect to concentration due to self-absorption of the scattered radiation.
At a pH of around 1 the dye is green with an absorption maximum at 620 nm while above pH 2 the dye is bright blue with a maximum at 595 nm. At pH 7 the dye has an extinction coefficient of 43,000 M −1 cm −1. [8] The different colours are a result of the different charged states of the dye molecule.
where λ is a wavelength, is the optical path length of the cuvette which contains the solution of the N compounds (chromophores), , is the molar absorbance (also known as the extinction coefficient) of the ith chemical species at the wavelength λ, c i is its concentration. When the concentrations have been calculated as above and absorbance ...
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. Hill coefficients vary ...