Please send message to my email if you response
cheng.luo at utu.fi
Mon Nov 18 14:25:20 EST 2002
> I have a GST-X fusion protein to be purified and crysatlized. The protein is
> very unstable after cleavage with thrombin, can be only stable in PMSF in
> pH8.0 for about 1 month, after concnetrated to 10mG/ml it is easy to be
> degraded again.
> The binding efficiency to gluthione sepahrose resin seemly depends on the
> protein expression and folding, which may be affected by some unknown
> factors, such as sonication?
> I am going to try to express the protein with E.coli BL21 (DE3) LysS. so to
> avoid the sonication.
> Someone may have such experience, and happy to share it.
> Cheng Luo, Ph.D.
> BTK/Medicity Research Laboratory
> University of Turku
> Tykistökatu 6 A
> FIN-20520, Turku
> Tel. +358 2 3338001
> Fax +358 2 3337000
> Email Cheng.Luo at utu.fi
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