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?

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

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?

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. :)