User:Nicole Bonan/Notebook/Chem 571 Lab Notebook/2015/09/30: Difference between revisions
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## 140uL of Assay Buffer | ## 140uL of Assay Buffer | ||
## 40uL of Assay Reagent | ## 40uL of Assay Reagent | ||
# We then pipetted this mixture into a 1mL quartz cuvette and took fluorescence measurements (excitation wavelength was 390nm and emission wavelengths | # We then pipetted this mixture into a 1mL quartz cuvette and took fluorescence measurements (excitation wavelength was 390nm and emission wavelengths were 400 to 650nm). | ||
===Brasford Analysis of Protease Degradation=== | ===Brasford Analysis of Protease Degradation=== |
Revision as of 21:56, 3 October 2015
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ObjectiveThe purpose of today's lab work is to:
ProtocolDr. Hartings's protocol for today is here. We are following his protocols for fluorescence and for the Bradford Assay. Fluorescence Analysis of Protease DegradationYesterday, we measured the fluorescence of all of our samples of alpha-chymotrypsin + lysozyme. Today, we finished the fluorescence measurements for the alpha-chymotrypsin blanks as follows:
Brasford Analysis of Protease DegradationData and AnalysisFluorescenceThe above figure shows the fluorescence of lysozyme in samples of varying concentrations of alpha-chymotrypsin as a function of the wavelength of incident light. The fluorescence of each sample was corrected for the blanks by subtracting the fluorescence of the blank from the fluorescence of the sample for every wavelength measured. Each curve on the graph represents a different concentration of alpha-chymotrypsin. The above image shows the fluorescence intensity of lysozyme as a function of the concentration of alpha-chymotrypsin that it is reacted with. Bradford Assay |