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mustafaismomo mustafaismomo
wrote...
Posts: 1
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12 years ago
Can anyone explain the SDS PAGE process in simple terms? Seem to have difficulty with understanding via my 5th Ed Cell Bio Textbook
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wrote...
Educator
12 years ago
Sure, these animals should help:

<a rel="nofollow" href="https://http://www.shsu.edu/~chm_tgc/sounds/flashfiles/GE.swf" target="_blank">https://http://www.shsu.edu/~chm_tgc/sounds/flashfiles/GE.swf</a>

<a rel="nofollow" href="https://http://oscar.iitb.ac.in/onsiteDocumentsDirectory/Electrophoresis%20Techniques-SDS%20and%20BN-PAGE/Electrophoresis%20Techniques-SDS%20and%20BN-PAGE/Courseassets/glossary.swf" target="_blank">https://http://oscar.iitb.ac.in/onsiteDocumentsDirectory/Electrophoresis%20Techniques-SDS%20and%20BN-PAGE/Electrophoresis%20Techniques-SDS%20and%20BN-PAGE/Courseassets/glossary.swf</a>

<a rel="nofollow" href="https://http://khayma.com/muhannad/flashat/flashat1/instanalysis/04.swf" target="_blank">https://http://khayma.com/muhannad/flashat/flashat1/instanalysis/04.swf</a>
wrote...
Staff Member
12 years ago
SDS-PAGE is the most widely used method for characterization of proteins and evaluation of their molecular weights and purity. Nearly all proteins are soluble in the presence of the anionic detergent sodium dodecyl sulfate (SDS). SDS binds to proteins with high affinity which confers a negative charge to the polypeptides and relaxes higher order protein structures. Complete disruption of tertiary and quaternary protein structures is essential to achieve protein separation according to molecular weight. This is accomplished by reduction of the inter- and intra-molecular disulfide bonds of polypeptides by the addition of agents such as dithiothreitol (DTT) or 2-mercaptoethanol and subsequent heating.
- Master of Science in Biology
- Bachelor of Science
wrote...
12 years ago
My prboelm was a wall until I read this, then I smashed it.
Val
wrote...
12 years ago
Bio_man has everything you need: yet just in case you need MORE:
SDS
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