Most of the interfering substances are commonly used as buffers in preparation of proteins (Lin & Liu 2006). Further, the Lowry assay is sensitive to variations in the quantities of tryptophan and tyrosine residues. According to Wang, Yang, and Du (2009), if the protein being assayed has got the unusual content of these compounds, a substitute should be used. Notably, the standard curve is linear in the 1 to 100 μg protein region. The absorbance is commonly achieved between 500 to 750 nm. Biuret technique: Protein determination through biuret technique is done using an ultraviolet wavelength of about 250-350nm (Aukkanit & Garnjanagoonchorn 2010). It shows the different spectrum with BSA and adsorption. Although in this experiment the maximum absorption was observed at 270, 280nm was preferred as the most appropriate wavelength. However, to obtain the highest sensitivity, the copper-iron concentration was required to be about 0.2% even though the NaOH concentration of less than 10% was the most desirable. Tartrate salt was used to enhance the solubility of copper ion. To arrive at different levels of concentration and absorption, the interpolation method was used. We determined the slope by taking two points along the straight line and calculate the change in y over the change in x. The Biuret And Lowry Assay Techniques.
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