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The Warburg–Christian method is an ultraviolet spectroscopic protein and nucleic acid assay method based on the absorbance of UV light at 260 nm and 280 nm wavelengths. Proteins generally absorb light at 280 nanometers due to the presence of tryptophan and tyrosine. Nucleic acids absorb more at 260 nm, primarily due to purine and pyrimidine ...
Specialized fluorescent dyes bind specifically to the substances of interest. A spectrophotometer is used in this method to measure the natural absorbance of light at 260 nm (for DNA and RNA) or 280 nm (for proteins). [5] [6] [7] [8]
Absorbance: Read at 280 or 215 nm. Can be very inaccurate. Detection in the range of 100 μg/mL to 1 mg/mL. Ratio of absorbance readings taken at 260/280 can indicate purity/contamination of the sample (pure samples have a ratio <0.8) Bradford protein assay: Detection in the range of ~1 mg/mL; Biuret Test Derived Assays:
The SI unit of molar absorption coefficient is the square metre per mole (m 2 /mol), but in practice, quantities are usually expressed in terms of M −1 ⋅cm −1 or L⋅mol −1 ⋅cm −1 (the latter two units are both equal to 0.1 m 2 /mol). In older literature, the cm 2 /mol is sometimes used; 1 M −1 ⋅cm −1 equals 1000 cm 2 /mol.
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.
Aromatic amino acids, excepting histidine, absorb ultraviolet light above and beyond 250 nm and will fluoresce under these conditions. This characteristic is used in quantitative analysis, notably in determining the concentrations of these amino acids in solution. [1] [2] Most proteins absorb at 280 nm due to the presence of tyrosine and ...
An absorption peak at 280 nm is visible due to aromatic amino acids which transfer their excitation energy to the green chromophore. The quantum yield of the green-emitting form of Eos is 0.7. [ 2 ] In the red shifted species, there are pronounced vibronic sidebands separate from the main peak at 533 nm and 629 nm in the excitation spectrum and ...
where is the fractional occupancy of the adsorption sites, i.e., the ratio of the volume V of gas adsorbed onto the solid to the volume of a gas molecules monolayer covering the whole surface of the solid and completely occupied by the adsorbate. A continuous monolayer of adsorbate molecules covering a homogeneous flat solid surface is the ...