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Isolation of proteins - 2 questions that I get stuck (Nov/28/2005 )

Hi everyone,

I have some questions in cell disruption which I cannot figure out. They are related to the step of isolation of proteins.
- How do you take care that the target protein will be as soluble as possible?
- How do you take care that the target protein will suppress? (salt fractionatating and solvent fractionating)

Could somebody work it out? Thanks in advance smile.gif



i'm not sure what you mean exactly when you say question in cell disruption and making sure you're protein is as soluble as possible. usually you need to play around with IPTG concentration and try to lower the induction temp a little to try and maximise the yeild of soluble protein. i am assuming you are doing iptg induction as there aren't any details.
as for salt fractionation, as far as i know it actually depends on the proteins solubility. if it's more soluble you might have to increase amm. sulphate percentages to get it to precipitate.
hope this helps. smile.gif


Thank you Soraya smile.gif, I think I understand what u have explained to me, it does help me wink.gif. Actually, I am doing a project on Protein in my course. I hope it's gonna be ok xP