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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 <[log in to unmask]> 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 <[log in to unmask]> wrote:
Dear All,
I am trying to probe the existence of a disulfide bond on the surface of my protein.
I have attempted Ellmanīs 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: [log in to unmask]
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-- 
Yuri Pompeu



--
*******************************************
Jacob Pearson Keller, PhD
Postdoctoral Associate
HHMI Janelia Farms Research Campus
email: [log in to unmask]
*******************************************