While most proteins have absorbance at 280 nm, some proteins also have absorbanc

Question

While most proteins have absorbance at 280 nm, some proteins also have absorbance in other regions of the UV-visible spectrum. One example, green fluorescent protein (GFP), has a major excitation peak at 395 nm. You use two different methods to measure the concentration of purified GFP: 1) absorbance at 395 nm using a spectrophotometer, and 2) Bradford assay. You obtain a different protein concentration from each method. Which method yields a higher concentration? Why do the two concentrations differ? Which measured value is more reliable for GFP quantification?

Explanation / Answer

the higher value of concentration wi be obtained in bradford assay as it may quantifies contamination also along with the pure sample. the more reliable method is spectrophotometer due to its calibration property of selectivity and specificity

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