Ionic interactions on Sephadex G-10
dmb618 at enh.nist.gov
Mon Jan 23 17:49:29 EST 1995
In article <3ffhms$m7s at dingo.cc.uq.oz.au>, J.Marcus at tpp.uq.oz.au
> : Ionic interactions on Sephadex G-10
>According to Phamacia, ionic interactions on Sephadex G-10
>are due to the fact that the cross-linked dextran chains contain
>a few terminal carboxyl groups; the gel will therefore act as a
>weak cation exchanger with very low capacity.
>To remove these effects, it is suggested to use an ionic strength
>of 50mM in the eluent buffer.
>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.
If you are trying to isolate your peptides salt-free, why not just a volatile
buffer such as ammonium acetate for your gel filtration and lyophilize the
fractions containing the peptides?
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