While researching for my project i came across the use of urea in PAGE and in some protein estimation studies... I know that Urea helps in the denaturation of the proteins but i am not getting why to use urea when we use beta-mercaptoethanol and heating for the denaturatioin of proteins.
I mean is there any other function attributed to the addition of the Urea or else if urea is better at denaturation????
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#2
vattav90
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Posted 03 April 2011 - 09:29 AM
25 views and not a single answer...is my question that silly!!!!! 
#3
DRT
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Posted 03 April 2011 - 05:05 PM
Because the proteins run differently in urea gels compared to SDS or native gels (urea preserves the native-like charge of the protein and primarily disrupts only H-bonds) it can be useful in some situations. Once upon a time it was common to have urea gradient through the gel in order to monitor protein denaturation but I don’t know if this is still done?
Plus it is sometimes possible to recover the activity post-gel with urea.
Plus it is sometimes possible to recover the activity post-gel with urea.
Edited by DRT, 03 April 2011 - 05:08 PM.
