User:Paul Rothenberg/Notebook/CHEM 571 Fall 2014/2015/03/18: Difference between revisions
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There was no visible colorimetric change in the solution. Fibers were still present at the end of the allotted reaction time. | There was no visible colorimetric change in the solution. Fibers were still present at the end of the allotted reaction time. | ||
==Protease Bradford - Control== | |||
250 μL samples of protease solutions in Tris/CaCl<sub>2</sub> buffer at the experimental concentrations (1 nM, 10 nM, 100 nM, and 1 μM) were combined with 200 mL of 1:4 (Bradford:Buffer) Bradford reagent and 550 mL of additional Tris/CaCl<sub>2</sub> buffer in order to determine the contribution of the protease protein to the Bradford absorbances observed in the AuNP fiber samples. | |||
'''Results''' | |||
[[Image:Control_Proteinase_K_Bradford_Absorbance.png]] | |||
[[Image:Control_Trypsin_Bradford_Absorbance.png]] | |||
[[Image:Control_Chymotrypsin_Bradford_Absorbance.png]] | |||
[[Image:Control_Thermolysin_Bradford_Absorbance.png]] | |||
Revision as of 14:44, 31 March 2015
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10 nM Chymotrypsin kineticsAnother in situ kinetics run. 104.1 µL of the dilute chymotrypsin stock was diluted with 2.896 mL of buffer for a final concentration of 10 nM when added to the fibers. The fibers and OceanOptics were prepared with the same protocol as previous kinetics runs. Results
There was no visible colorimetric change in the solution. Fibers were still present at the end of the allotted reaction time. Protease Bradford - Control250 μL samples of protease solutions in Tris/CaCl2 buffer at the experimental concentrations (1 nM, 10 nM, 100 nM, and 1 μM) were combined with 200 mL of 1:4 (Bradford:Buffer) Bradford reagent and 550 mL of additional Tris/CaCl2 buffer in order to determine the contribution of the protease protein to the Bradford absorbances observed in the AuNP fiber samples. Results
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