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  2. Molar absorption coefficient - Wikipedia

    en.wikipedia.org/wiki/Molar_absorption_coefficient

    The absorbance of a material that has only one absorbing species also depends on the pathlength and the concentration of the species, according to the Beer–Lambert law =, where ε is the molar absorption coefficient of that material; c is the molar concentration of those species; ℓ is the path length.

  3. Molar concentration - Wikipedia

    en.wikipedia.org/wiki/Molar_concentration

    Molar concentration or molarity is most commonly expressed in units of moles of solute per litre of solution. [1] For use in broader applications, it is defined as amount of substance of solute per unit volume of solution, or per unit volume available to the species, represented by lowercase c {\displaystyle c} : [ 2 ]

  4. Absorbance - Wikipedia

    en.wikipedia.org/wiki/Absorbance

    Absorbance is defined as "the logarithm of the ratio of incident to transmitted radiant power through a sample (excluding the effects on cell walls)". [1] Alternatively, for samples which scatter light, absorbance may be defined as "the negative logarithm of one minus absorptance, as measured on a uniform sample". [2]

  5. Nucleic acid quantitation - Wikipedia

    en.wikipedia.org/wiki/Nucleic_acid_quantitation

    The secondary benefit of using spectrophotometric analysis for nucleic acid quantitation is the ability to determine sample purity using the 260 nm:280 nm calculation. The ratio of the absorbance at 260 and 280 nm (A 260/280) is used to assess the purity of nucleic acids.

  6. Determination of equilibrium constants - Wikipedia

    en.wikipedia.org/wiki/Determination_of...

    where l is the optical path length, ε is a molar absorbance at unit path length and c is a concentration. More than one of the species may contribute to the absorbance. In principle absorbance may be measured at one wavelength only, but in present-day practice it is common to record complete spectra.

  7. Bradford protein assay - Wikipedia

    en.wikipedia.org/wiki/Bradford_protein_assay

    The increase of absorbance at 595 nm is proportional to the amount of bound dye, and thus to the amount (concentration) of protein present in the sample. [ 6 ] Unlike other protein assays, the Bradford protein assay is less susceptible to interference by various chemical compounds such as sodium, potassium or even carbohydrates like sucrose ...

  8. Benesi–Hildebrand method - Wikipedia

    en.wikipedia.org/wiki/Benesi–Hildebrand_method

    The two parameters, K or ε are determined by using the Solver module a spreadsheet, by minimizing a sum of squared differences between observed and calculated quantities with respect to the equilibrium constant and molar absorbance or chemical shift values of the individual chemical species involved.

  9. Ellman's reagent - Wikipedia

    en.wikipedia.org/wiki/Ellman's_reagent

    This reaction is rapid and stoichiometric, with the addition of one mole of thiol releasing one mole of TNB. The TNB 2− is quantified in a spectrophotometer by measuring the absorbance of visible light at 412 nm, using an extinction coefficient of 14,150 M −1 cm −1 for dilute buffer solutions, [4] [5] and a coefficient of 13,700 M −1 cm −1 for high salt concentrations, such as 6 M ...