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SDS and Native page electrophoresis

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satty

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Hi guys,
What is the difference between sds and native( I kindoff know the basic things like denaturing,functional activity is maintained in native) but i am looking for a moreadvanced difference between the two and also
In SDS PAGE the relative complexity of the sample compared to Native PAGE (i.e. number of bands). Why is there a difference? tho we have the same sample in both the systems?

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Posted Apr 27, 2007, 12:38 PM
guy

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Hi,
I am enclosing a link, read it and I hope it will answer some of your questions. If you still got some with no answer, write and we will try to help.
Guy

http://www.piercenet.com/Proteomics/browse.cfm?fldID=21518847-2D72-475F-A5B9-B236EC5B641E#native%20page

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Posted Apr 27, 2007, 18:42 PM
satty

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thank you guy for yr timely help.What abt the answer to my second question? why are there so many bands in sds and not in native page?

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Posted Apr 28, 2007, 3:01 AM
Gibacht

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As a example with a IgG, it has a mol weight of about 190 KD, with SDS PAGE you get 2 chains with about 80 KD that makes 160 KD, and a small chain with about 30 KD this summs up to 190 KD.
So with SDS PAGE you have 3 bands and with a summ of 190KD, and with native PAGE one Band with 190 KD, because it is not reduced.
I hope this helps you. :)

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Posted May 27, 2008, 5:50 AM
qinglongyanyuedao

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satty said:
thank you guy for yr timely help.What abt the answer to my second question? why are there so many bands in sds and not in native page?


in SDS gel, your proteins are denatured, and all proteins appeared to be bands
well, in a native gel, your proteins are still in their native format, i.e., they are still in the protein complex they belong,
so, to your question, a native gel separates native protein complexes, and SDS gel separates individual proteins.

let's say that if you have ten proteins in a complex, which will be separated on a native gel as one band, but will be 10 on a sds gel

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UGGGCUAAUGGU*CAAAUUGCCAACGGC

Posted Jul 18, 2008, 11:22 AM
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