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 marvin.biologie.uni-konstanz.de> stephan.witte at uni-konstanz.de (Stephan Witte) writes:
> >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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