Even so, it should run somewhat differently, and probably visibly on
SDS-PAGE. Even a single phosphorylation changes mobility, and I think I
remember having seen intramolecular disulfides change mobility (anyone else
have experience on this?)

JPK

On Wed, Feb 6, 2013 at 10:33 PM, Yuri <yuri.pom...@ufl.edu> wrote:

> **
>
> The disulfide bond is intramolecular. I do not have reasons to believe it
> is cross linking my protein
>
>
>
>
>
> On Wed, 6 Feb 2013 22:16:36 -0500, Jacob Keller wrote:
>
> Couldn't you just run reducing/non-reducing SDS-PAGE lanes and see the
> difference?
> JPK
>
> On Wed, Feb 6, 2013 at 11:10 AM, Yuri Pompeu <yuri.pom...@ufl.edu> wrote:
>
>> Dear All,
>> I am trying to probe the existence of a disulfide bond on the surface of
>> my protein.
>> I have attempted EllmanĀ“s and my results were not as clear as I would
>> have hoped for.
>> I am not a sulfur/cysteine chemist and would appreciate the advice on
>> what experiments to try!
>> Thanks a bunch
>> YAP
>
>
>
> --
> *******************************************
> Jacob Pearson Keller, PhD
> Postdoctoral Associate
> HHMI Janelia Farms Research Campus
> email: j-kell...@northwestern.edu
> *******************************************
>
>
>
> --
> Yuri Pompeu
>
>


-- 
*******************************************
Jacob Pearson Keller, PhD
Postdoctoral Associate
HHMI Janelia Farms Research Campus
email: j-kell...@northwestern.edu
*******************************************

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