User:Keyun Wang/Notebook/Experimental Biological Chemistry I/2012/11/28: Difference between revisions
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* From table above, it can be concluded that resuspension happened faster in solutions with Tris buffer pH 10.0 then solutions with Tris buffer pH 8.0. | * From table above, it can be concluded that resuspension happened faster in solutions with Tris buffer pH 10.0 then solutions with Tris buffer pH 8.0. | ||
* It was observed that resuspension time needed was must shorter in Tris buffer with pH 10.0 than in Tris buffer with pH 8.0. Possible reason for this result can be due to the high pH introduced by Tris buffer at pH 10.0 is much higher than the isoelectric point in ADA protein. This allows proteins to become negatively charged faster. Ions in buffer with stronger ionic strength can dissociate in solution and break apart the nanoparticle aggregation by interacting with the net negative charge on protein. | |||
* On the other side, at pH 8.0, less ADA proteins make the transition in time in order to take on a whole negative charge. As a result, not all ions would be able to form charge-charge interaction with the proteins, and in total delaying the process for protein aggregation breakdown, slowing down the time for complete resuspension. | |||
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Revision as of 21:11, 7 December 2012
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Purpose
Procedure for Running Au/ADA samples on UV-vis Spectrophotometer
60-70-80-90-100-110-120-130-140-150
Results for Running Au/ADA samples on UV-vis Spectrophotometer
Procedure for Running Au/ADA samples on Atomic Absorption Spectrometer
5-8-10-15-20-25-30-40
Results for Running Au/ADA samples on Atomic Absorption Spectrometer
Absorbance = 0.0153 * Concentration + 0.045
Procedure for Au/ADA Resuspension in Tris Buffer
Results for Au/ADA Resuspension in Tris Buffer
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