User:Noah Benjamin/Notebook/Experimental Biological Chem/2011/09/14: Difference between revisions
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[[Image:MolarAbsorbtivity.png]] | [[Image:MolarAbsorbtivity.png]] | ||
Protein molar absorbtivity calculated using the equation "molar abs. = absorbance / (pathlength x concentration)". Pathlength used was 0.01 meters. Concentration used was 0.000002g/mL (2µg/mL) of protein. | |||
==Notes== | ==Notes== | ||
Revision as of 05:56, 20 September 2011
 Biomaterials Design Lab
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ObjectiveDescription41 µL of Bovine Serum Albumin EMD Biomedicals Inc.; Fraction V) and 595.9 µL of distilled water were combined to create 6 mL of a 9.97 µg/mL stock solution. 6 disposable cuvettes were filled with 800, 600, 400, 300, 200, and 100 µL of the BSA stock solution respectively. Each cuvette was then filled with 200 µL of Bradford Reagent (BioRad Laboraties Inc.) and enough distilled water to produce a final solution volume of 1 mL. 10 µL of Maltose binding protein (generously provided by Dr. Hardings) was combined with 990 µL of distilled water as a stock solution. 200 µL of this protein stock solution was combined in a cuvette with 200 µL of Bradford Reagent and 600 µL of distilled water. Blank controls were then prepared by preparing two cuvettes of 200 µL Bradford Reagent and 200 µL of the protein stock solution respectively, and adding 800 µL of distilled water to each. UV-Visible spectra analyses were then taken of each cuvette using a UV-2550 Spectrophotometer (Shimadzu). The spectra were analyzed and calibration curves were prepared. Data
NotesThis area is for any observations or conclusions that you would like to note.
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