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

hanson via proteins%40net.bio.net (by hanson At quick.net)
Wed Jan 10 23:25:23 EST 2007


"Bob" <bbx107.XYZ At excite.XYZ.com> wrote in message
news:a49bq2lve6k3skf7thuqronoo2csh4hq3a At 4ax.com...
>
[Bob]
> If you have it at fairly high concentration in an oxidizing
> environment (air), and the Cys are exposed, one would expect that.
> Solutions include keeping the conc low, avoiding oxidation -- and
> reducing the dimers back to monomers, say with mercaptoethanol.
>
[hanson]
Interesting. Are you basically telling here that the oxidized/dimer of
Cysteine, now Cystine: HOOC(NH2)C-CH2-S-S-CH2-C(NH2)COOH
together with 2 HS-CH2-CH2-OH disproportionates/redoxes into
 2 HS-CH2-C(NH2)COOH  and HO-CH2-CH2-S-S-CH2-CH2-OH.

Does HSEtOH work as a reducer for all -S-S- molecules in biologial
systems?








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