Ionic interactions on Sephadex G-10

Robert Jordan jordan at mbcrr.harvard.edu
Tue Jan 17 14:28:02 EST 1995


In article <3ffhms$m7s at dingo.cc.uq.oz.au>, J.Marcus at tpp.uq.oz.au (John
Marcus) wrote:
> 
> I want to desalt low molecular weigth peptides (1000-5000Da) using
> G-10 Sephadex.  My problem is that I don't want any buffer at all 
> in the eluent.  The proteins I am desalting are quite basic so I fear
> that some might interact with the column packing if I were to totally
> do away with buffer.  Ideally, I would like to use straight deionized
> water to elute the proteins from the column.
>  
John,

You might want to consider reverse phase HPLC. Small peptides are eluted
with a gradient of acetonitrile in H20 in the presence of 0.03%
Triflouroacetic acid. These solvents are volitile and can be evaporated
off. The peptide can be resuspened in any solvent you want.

Rob J.



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