Hi,
I've just ran a SDS-PAGE gel with diferent proteins diluted in a buffer containing BSA. In the samples were I added DTT the BSA band did not ran as far as the same sample without DTT. What is the explanation for that?
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Posted 15 June 2011 - 09:54 PM
protchem, on 15 June 2011 - 05:53 AM, said:
Hi,
I've just ran a SDS-PAGE gel with diferent proteins diluted in a buffer containing BSA. In the samples were I added DTT the BSA band did not ran as far as the same sample without DTT. What is the explanation for that?
I've just ran a SDS-PAGE gel with diferent proteins diluted in a buffer containing BSA. In the samples were I added DTT the BSA band did not ran as far as the same sample without DTT. What is the explanation for that?
Hola , with reducer the molecule is missfolded and have more difficlty to cross the acrylamide matrix; without the folded protein is more structurated, more compact and run a bit fast. Wait for the opinion of more forers that if I¨m wrong they give you a more specific explanation. Good luck
