[Protein-analysis] Re: equilibrium const for disulfide bond formation

Bill Penrose via proteins%40net.bio.net (by penrose At iit.edu)
Thu Jan 11 00:04:27 EST 2007


juicym... At mailinator.com wrote:
>
> This is a pretty simple question; however I can't seem to find an
> answer to it.

Dimerization is almost a given under your conditions.

There was a time, in the paleolithic days of biochemistry, that newly
isolated proteins were routinely kept in buffers containing
mercaptoethanol (2 to 10 mM) until you knew better. Later,
dithiothreitol (Cleland's Reagent) came along, which is a stronger
reducing agent for stubborn cases, and didn't stink quite as much.

Of course, any labeling you plan to do on the cyse will be completely
derailed until you get rid of all the added thiols by dialysis.
Afterward, keep the protein under nitrogen and label as soon as
possible. 

Dangerous Bill



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