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 *******************************************