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  2. 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 ...

  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. Nucleic acid quantitation - Wikipedia

    en.wikipedia.org/wiki/Nucleic_acid_quantitation

    In essence, the Beer Lambert Law makes it possible to relate the amount of light absorbed to the concentration of the absorbing molecule. The following absorbance units to nucleic acid concentration conversion factors are used to convert OD to concentration of unknown nucleic acid samples: [5] A260 dsDNA = 50 μg/mL A260 ssDNA = 33 μg/mL

  5. 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]

  6. Calibration curve - Wikipedia

    en.wikipedia.org/wiki/Calibration_curve

    A calibration curve plot showing limit of detection (LOD), limit of quantification (LOQ), dynamic range, and limit of linearity (LOL).. In analytical chemistry, a calibration curve, also known as a standard curve, is a general method for determining the concentration of a substance in an unknown sample by comparing the unknown to a set of standard samples of known concentration. [1]

  7. Variable pathlength cell - Wikipedia

    en.wikipedia.org/wiki/Variable_pathlength_cell

    Variable pathlength absorption spectroscopy uses a determined slope to calculate concentration. As stated above this is a product of the molar absorptivity and the concentration. Since the actual absorbance value is taken at many data points at equal intervals, background subtraction is generally unnecessary.

  8. Enzyme assay - Wikipedia

    en.wikipedia.org/wiki/Enzyme_assay

    The rate of a reaction is the concentration of substrate disappearing (or product produced) per unit time (mol L −1 s −1).. The % purity is 100% × (specific activity of enzyme sample / specific activity of pure enzyme).

  9. Lowry protein assay - Wikipedia

    en.wikipedia.org/wiki/Lowry_protein_assay

    The concentration of the reduced Folin reagent (heteropolymolybdenum Blue) is measured by absorbance at 660 nm. [7] As a result, the total concentration of protein in the sample can be deduced from the concentration of tryptophan and tyrosine residues that reduce the Folin–Ciocalteu reagent. The method was first proposed by Lowry in 1951.