If the molar absorptivity at a specific wavelength is known for a protein, it is pretty easy to determine its concentration simply by measuring its absorbance and using Beers law. Based on the following information, spectrophotometrically determine the concentration (in mg/mL) of a solution of the protein lysozyme. mL -the molar absorptivity at 280 nm (converted for units of mg/mL) is E 280 = 0.243- mg · cm -the absorbance of a solution of lysozyme is 0.923 when the path length is 1 cm.

Principles of Modern Chemistry
8th Edition
ISBN:9781305079113
Author:David W. Oxtoby, H. Pat Gillis, Laurie J. Butler
Publisher:David W. Oxtoby, H. Pat Gillis, Laurie J. Butler
Chapter20: Molecular Spectroscopy And Photochemistry
Section: Chapter Questions
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If the molar absorptivity at a specific wavelength is known for a protein, it is pretty easy to
determine its concentration simply by measuring its absorbance and using Beers law. Based on
the following information, spectrophotometrically determine the concentration (in mg/mL) of a
solution of the protein lysozyme.
mL
-the molar absorptivity at 280 nm (converted for units of mg/mL) is E280 =0.243
mg · cm
-the absorbance of a solution of lysozyme is 0.923 when the path length is 1 cm.
Transcribed Image Text:If the molar absorptivity at a specific wavelength is known for a protein, it is pretty easy to determine its concentration simply by measuring its absorbance and using Beers law. Based on the following information, spectrophotometrically determine the concentration (in mg/mL) of a solution of the protein lysozyme. mL -the molar absorptivity at 280 nm (converted for units of mg/mL) is E280 =0.243 mg · cm -the absorbance of a solution of lysozyme is 0.923 when the path length is 1 cm.
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