Vernon,
Have a look at the paper by Getz,et al.
"A Comparison between the sulfhydryl reductants TCEP and DTT for use in Protein
Biochemistry" Anal Biochem (1999)273,73-80.
Sandy.
On 15 Nov 00 08:25:16 -0500 VERNON SHOUP <vernon.shoup@regpha.com> wrote:
> In one of our processing steps for a protein drug, we will be using TCEP to reduce a disulfide bond. We do have to be aware of any potential side reactions. Is anyone aware of any side reactions when proteins are treated with TCEP?
>
> To prompt discussion, here are a couple of possibilities:
>
> 1. Incomplete reduction would produce a mixture of sulfhydryl groups and disulfide bonds, and might promote disulfide scrambling.
>
> 2. Suppose there were some methionine sulfoxide residues in the protein, due to previous oxidation. Would the reagent reduce those back to methionine?
>
> Vernon
>
> Vernon A. Shoup
> Regeneron Pharmaceuticals
> Rensselaer, NY
>
> (518)488-6012
> vernon.shoup@regpha.com
>
----------------------
Alex Carne,
Head of Protein Characterization,
Institute of Cancer Research,
Chester Beatty Labs.,
237 Fulham Road,
London SW3 6JB, UK.
Tel: +44(0)207 878 3815 (Office)
Tel: +44(0)207 970 6003 (Lab)
Fax: +44 (0)207 352 3299
E-mail: sandyc@icr.ac.uk
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