Why is the reduced protein (with 2-ME) placed higher than the non-reduced one in SDS-PAGE?
Dear Hossein Ansariniya
the reason why a reduced protein generally run slower respect a non reducing protein is because the reduced protein, which miss intramolecular S-S bonds is less compact (unfolded) and therefore the hydrodinamic radius increase.
An exception is possible when the cysteines are involved in intermolecular S-S bonds that in absence of reducing agent can drive to detection in SDS page of the aggregates as dimer, multimer, oligomers.
at minute 7'50'' of the following video
https://www.blogger.com/video.g?token=AD6v5dyp2LLPNQObE-O7xpUxV02oGcx4RQ0mfxIRjK1x1YHBCYw3Av9JZTXdeO6JXLu6wl6Cd2omOIASqXY7BDpDcvlzrJ8fQSoqXnMyd5Fqcc3vRe-1JCCyISDv7Y-UACmOPKhEV6M
on my blog (ProteoCool) you can see a more detailed explanation about it.
best
Manuele
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