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Laemmli U. K.

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Q: Who discovered SDS PAGE electrophoresis?
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Why is denaturing sds-page used for running sds-page electrophoresis of egg-white lysozyme and not non-denaturing page?

may be because of toomany disulfide linkages


What are the different parts of electrophoresis?

SDS-PAGE AGAROSE CAPILLARY SEQUENCING TO NAME A FEW


What is the advantage of adding SDS to gel electrophoresis?

SDS PAGE electrophoresis is an important method in the separation of proteins. it can be use to identify and isolate proteins aswell as determine if a protein solution is pure or contaminated


Is DNA smaller or bigger than a protein?

Let's put it this way, we know that electrophoresis is a test for the sizes of the fragments of DNA molecules while SDS-page is a test of the size of protein molecules. If you use electrophoresis to test the differences of protein, there will not be any bands as all the protein will travel to the end of SDS-page. Therefore, we can conclude that the pores of electrophoresis is much more larger than SDS-page. Since electrophoresis has larger pores than SDS-page, it also shows that overall DNA is larger than protein in size.


What method could you use to further separate two bands from the same protein fraction after SDS-PAGE?

Electrophoresis is the method that could be used to further separate two bands from the same protein fraction after SDS-PAGE.


What is vertical gel electrophoresis unit?

Samole moves from top to bottom is called vertical gel system, for example a SDS PAGE gel.


DNA fragments can be separated and analyzed by?

Pulse field gel electrophoresis is used to separate DNA fragments by their size.


What is SDS phage?

there is nothing like SDS phage but... 1. SDS is a well know detergent used to denature proteins before electrophoresis called SDSPAGE. 2. phage (bacteriophage) is a virus that infects the bacteria which contains eother DNA or RNA. SDS PAGE can be used to determine the phage proteins which u can call SDSPAGE of phage.


What is sds-page used for?

SDS - PAGE is apparently used to seperate proteins. The proteins are by nature different sizes. SDS works as a stabilizer by separating proteins according to similar forms.


What is the function of glycine in sds page?

glycine molecular weight high so mobility also high so using in SDS PAGE


Why p53 is run as 53 kda on sds page?

Due to many proline residues it migrates slower on sds page and appears heavier than it is.


What are the drawbacks of sds page?

The major drawback is that treatment with SDS denatures the protein, meaning you are not looking at it in its natural state.