Abstract
A modified method of SDS-polyacrylamide gel electrophoresis for the efficient separation of low molecular weight proteins (ranging 1.4–10 kDa, containing di-sulfide bonds) without frowning, smiling and diffusion is described. SDS-polyacrylamide and tricine gel electrophoresis are considered as standard approaches for low molecular weight protein separation, despite frowning, smiling and diffusion problems. These methods are inefficient and confusing as Coomassie brilliant blue stained low molecular weight protein bands are difficult to identify since proteins get diffused and, it is difficult to identify as proteins. The method developed offers a solution to the existing problem and is more suitable for the efficient separation of low molecular weight proteins with high resolution (with di-sulfide bonds).
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More From: International Journal of Peptide Research and Therapeutics
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