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Enzyme activity as given in katal generally refers to that of the assumed natural target substrate of the enzyme. Enzyme activity can also be given as that of certain standardized substrates, such as gelatin, then measured in gelatin digesting units (GDU), or milk proteins, then measured in milk clotting units (MCU). The units GDU and MCU are ...
Adjust the spectrophotometer to a wavelength of 595 nm, using the tube which contains no protein (blank). Wait 5 minutes and read each of the standards and each of the samples at 595 nm wavelength. Plot the absorbance of the standards vs. their concentration. Compute the extinction coefficient and calculate the concentrations of the unknown ...
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.
In biochemical experiments, a chemical and/or physical property is chosen and the procedure that is used is specific to that property to derive more information about the sample, such as the quantity, purity, enzyme activity, etc. Spectrophotometry can be used for a number of techniques such as determining optimal wavelength absorbance of ...
The absorbance of this colored solution can be quantified by measuring at a certain wavelength (usually between 500 and 600 nm) by a spectrophotometer. The degree of light absorption is dependent on the degree of formazan concentration accumulated inside the cell and on the cell surface.
The composition of a mixture of N absorbing species can be found by measuring the absorbance at N wavelengths (the values of the molar absorption coefficient for each species at these wavelengths must also be known). The wavelengths chosen are usually the wavelengths of maximum absorption (absorbance maxima) for the individual species.
This compound is chosen because the enzyme facilitates the reaction with hydrogen peroxide, turning it into a green and soluble end-product. Its new absorbance maximum of 420 nm light (ε = 3.6 × 10 4 M –1 cm –1) [2] can easily be followed with a spectrophotometer, a common laboratory instrument.
Absorbance detection has been available in microplate readers for more than 3 decades and is used for assays such as ELISA assays, protein and nucleic acid quantification or enzyme activity assays [2] (i.e. in the MTT assay for cell viability). [3]