The major difference between native PAGE and SDS PAGE is that in native PAGE the proteins migrate by charge to mass ratio and in SDS PAGE the proteins migrate exclusively because of the mass...
This is because SDS being a anionic detergent, will impart a series of negative charge in the protein molecule making them linear negatively charged molecules. The charge being all the same, i.e., negative, the proteins then migrate due to their mass...
You may take a look at the following links, which i think solve your problem.
http://in.answers.yahoo.com/question/index?qid=20061024045946AAdyRkJ
https://www.researchgate.net/post/Can_anyone_detail_the_differences_between_Native_PAGE_and_SDS-PAGE
Best of luck dear.............
When you use a native PAGE the protein pattern that you obtain is resolved by chemical and physical properties of the protein. So the lower band of the pattern could not represent protein at lower molecular size as SDS-PAGE but protein with high negative charged. The native PAGE is used, in comparison with SDS one , for example, if you want know if a purified protein has subunit.
The molecular weight could be estimated with SDS PAGE.In SDS PAGE samples are treated in order to have a uniform charge, so electrophoretic mobility in SDS PAGE depends mainly on size. SDS PAGE is carried out in the presence SDS ,SDS disrupts the tertiary structure of the protein to produce a linear chain which is negatively charged. non-denaturing sample used in native page. which maintains both the proteins’ secondary structure and native charge density.
The major difference between native PAGE and SDS PAGE is that in native PAGE the proteins migrate by charge to mass ratio and in SDS PAGE the proteins migrate exclusively because of the mass...
This is because SDS being a anionic detergent, will impart a series of negative charge in the protein molecule making them linear negatively charged molecules. The charge being all the same, i.e., negative, the proteins then migrate due to their mass...
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