tb at pharmexa.com ("Tomas Bratt") wrote:
> Dear discussion group,
>> I agree with you that misfolded proteins will probably run with
>a MW close to a native structure or they will form aggregates or
>polymers. But gelfiltration will give an answer if there are misfolded
>proteins because of peak broadening and/or polymeric forms. If the
>native protein is dimer or higher -mer it is also worth doing gel
>filtration as misfolded variants probably will not form the same -mer
>form. For a more general applicable separation see the article below or
>others like it that uses RP-HPLC, an efficient and powerful technique
>that could be used for many different proteins, just as Rick wanted.
> Good luck
> Tomas
>> Preparative isolation of recombinant human insulin-like growth
>factor 1 by reversed-phase high-performance liquid chromatography.
>=09
> Olson CV, Reifsnyder DH, Canova-Davis E, Ling VT, Builder SE.
> J Chromatogr A 1994 Jul 22;675(1-2):101-12
Problem with RP is that it is only useful for small/sturdy proteins
because it readily denatures many others (too strong binding).
DK
