At equilibrium, the cyanate concentration of 8M urea is about 0.02M.
Cyanate reacts with amino groups on proteins, Stark et al JBC 235, 3177,
1960. The cyanate breaks down in acid to CO2 and ammonium in acid. It can
also be avoided by using freshly crystallized urea or deionizing the urea.
The reactions of cyanate with proteins is summarized in Methods Enzymol
XI, p 590 1967.
Ken
Kenneth A. Walsh
E.W.Davie/ZymoGenetics Chair of Biochemistry
Box # 357350
University of Washington
Seattle WA 98195
walsh@u.washington.edu
Phone 206-543-1768
FAX 206-685-9231
On Mon, 22 Jun 1998, Harry Whatley wrote:
> ABRFers --
>
> It seems to be widely accepted that urea can modify proteins,
> particularly if the urea is old or has been heated. I have been unable
> to find any references to how this takes place.
>
> Can anyone point me to references on this subject? Also, is anyone
> aware of UV induced reactivity of urea?
>
> Thanks,
> Harry
>
> ^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^
> ------ __o
> ---- _ \<,_ I'd rather be biking!
> --- (_)/ (_)
> ---------------------------------------
> http://www.neptune.net/~whatley/
> =======================================
>
>
> ______________________________________________________
> Get Your Private, Free Email at http://www.hotmail.com
>
>