renaturation of proteins expressed in inclusion bodies

Brian A. Hollander afn08460 at FREENET.UFL.EDU
Wed Apr 19 01:09:58 EST 1995

I don't know precisely how much renaturation goes on but Harris et al. 
(1991) J. Neurosci. Res. 30:47. have purified fusion proteins from 
inclusion bodies by dissovling thm in 6M urea in buffer and subsequent 
DEAE chromatography. They assayed these proteins with Abs on western 
blots, where we don't really know how much renaturation takes place. Still 
many of the same Abs recognize the antigens in situ. I have used a 
similar procedure to isolate fusion proteins which can act as kinase 
substrates in vitro after dialysis.


On Tue, 18 Apr 1995, Tom Thatcher wrote:

> In <stephan.witte-180495095738 at> stephan.witte at (Stephan Witte) writes:
> >Hi,
> >Has anyone a reliable procedure (protocol and/or reference) for the
> >renaturation of proteins expressed in e. coli as inclusion bodies?

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