Hi,

Thank you for all replies. 

Sincerely
Debajyoti



On Mon, 25 Aug 2008 Artem Evdokimov wrote :
>If your protein precipitates at low ionic strength you may want to establish
>what concentration of salt does it tolerate (by slowly diluting a fraction
>of your pool with water just until you see precipitation) then try to adjust
>your cation exchange conditions so that you load with enough salt to keep
>the protein happy, then elute with higher salt concentration. You may want
>to adjust the pH of your buffer to be lower - usually this helps keep things
>in solution with basic proteins such as yours. In general you don't *have*
>to dialyze prior to ion exchange - dilution works just as well.
>
>
>
>Imidazole and histidine are pretty much the same in terms of protein
>behavior, at least in my experience. Both of them can cause 'apparent'
>protein degradation - if you take a sample of your protein with histidine or
>imidazole still in it, then boil it with the gel loading buffer you can get
>fake proteolysis (i.e. only in the boiled sample). It does not happen with
>every protein, but it does happen (some weird chemistry involving the
>imidazole ring at high temp. no doubt).
>
>
>
>Artem
>
>   _____
>
> From: CCP4 bulletin board [mailto:[EMAIL PROTECTED] On Behalf Of
>Debajyoti Dutta
>Sent: Sunday, August 24, 2008 3:21 AM
>To: [email protected]
>Subject: Re: [ccp4bb] protein degradation
>
>
>
>
>Hi again,
>
>Thank you for all you have replied. I suspect the sonnication for such a bad
>result. I am just wondering if I can use Histidine instead of Imidazole and
>then buffer exchange to go for Cation exchanger.
>Does Imidazole had any bad effect in protein. I have experienced that the
>protein cannot sustain low salt and get ppt during dialysis.
>
>Sincerely
>Debajyoti Dutta
>
>
>On Sat, 23 Aug 2008 Artem Evdokimov wrote :
> >Hi,
> >
> >
> >
> >If you are plagued by 'generic' proteolysis, it is not likely that changing
> >buffers from TRIS to phosphate will help reduce the breakdown. You may want
> >to ask yourself several key questions regarding the breakdown:
> >
> >
> >
> >1.     is it proteolysis or abortive translation?
> >2.     is it happening during expression or post-lysis?
> >3.     is it exoproteolysis or endo- (or both)? Which terminus is more
> >affected?
> >
> >
> >
> >If you have abortive translation or alternate transcription/translation
> >starts, you should examine the DNA/RNA sequence of your gene closely -
> >sometimes you can tell (e.g. beginning of the gene is peppered with
> >methionines and S-D sequences)
> >
> >
> >
> >If you have proteolysis during expression, it sometimes can be alleviated
>or
> >even eliminated by changing expression conditions (temperature and richness
> >of media seem to be key - this summer we had exactly this kind of a
> >situation where expression at 37C for 4 hours gave more total protein than
> >expression at 20C overnight, however the 37C protein was significantly
> >'busted up' whereas the 20C was essentially intact).
> >
> >
> >
> >If you have proteolysis during cell lysis you may be able to reduce its
> >extent by means of at least the following (not a complete list by any
> >means!):
> >
> >
> >
> >a)      lyse and process the cells on ice or even in liquid nitrogen (see
> >some previous posts regarding mortar-and-pestle LN2 lysis). Avoid
>sonication
> >or other forms of mechanical lysis in-liquid as they all generate heat
> >(detergent lysis or French press may be safe alternatives)
> >
> >b)      make an effort to lyse the cells and complete primary extraction as
> >fast as possible (for example, in an extreme case you can forego the lysate
> >clarification step - high-flow IMAC resins can tolerate complete crude
> >lysate in batch mode or sometimes even on a column).
> >
> >c)      use protease inhibitors (can be somewhat expensive)
> >
> >
> >
> >If you can figure out which end of the protein is affected (or perhaps its
> >lysis of an interdomain linker, exposed loop, etc.) you may be able to
> >re-design the construct to avoid this. Presumably the fact that your
>protein
> >can be extracted via the His6 tag means that the end with the tag is intact
> >(or at least enough of it is intact to make purification possible).
> >Therefore it may be interesting to switch the tag to the other end - you
>may
> >get lucky.
> >
> >
> >
> >If you cannot afford the (expensive) commercial protease inhibitor
> >cocktails, you may be able to get away with using the 'old basics' such as
> >benzamidine, PMSF (AEBSF), and EDTA/EGTA or phenantroline. Yes, you won't
>be
> >able to use IMAC together with EDTA - but you can always do cation exchange
> >first (protein with pI of 10!!!) in EDTA, then polish it up with IMAC etc.
> >If your protein is really pI 10, it should bind to CM-sepharose in buffer
> >with pH as high as 8, which is essentially a guarrantee that your protein
> >will be almost alone in the extracted material - you wil likely see a
> >ribosomal p10 protein that's about pI 11 - and that's it. Remember that if
> >you go this way, you should avoid using lysozyme for cell lysis since HEWL
> >is mighty basic itself.
> >
> >
> >
> >Good luck,
> >
> >
> >Artem
> >
> >
> >
> >  _____
> >
> > From: CCP4 bulletin board [mailto:[EMAIL PROTECTED] On Behalf Of
> >Debajyoti Dutta
> >Sent: Friday, August 22, 2008 6:16 PM
> >To: [email protected]
> >Subject: [ccp4bb] protein degradation
> >
> >
> >
> >
> >Hi,
> >
> >This is going to be an off topic question concerning this community. I have
> >a protein 6XHis tagged. When retrieved from the Ni-NTA column with
>imidazole
> >found to be degraded, appears like a deep band with other bands (touching
> >each other below the main band) in SDS PAGE. The protein is a DNA binding
> >(pI~ 10) and Tris-Hcl buffer is used with 10% glycerol and 300mM NaCl. for
> >purification. Does Phosphate buffer do any help in stopping the
>degradation.
> >
> >All suggestions are welcome. Thank you for your reply in advance.
> >
> >Sincerely
> >Debajyoti Dutta
> >
> >
> >
> >
> >
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