Biotin - Streptavidine - How to destroy this complex? (Sep/09/2008 )

Hi, we are planning to do affinity chromatography with biotin labeled peptides and sepharose-bound streptavidin.
But release of biotinylated peptide from the streptavidin-based reagents might be big problem, due to the extraordinary stability of this complex. Does anybody know the conditions how to unbound biotin from streptavidin?
Thanks.

-Brouk-

QUOTE (Brouk @ Sep 9 2008, 05:51 AM)

70°C clear water for 1 min, if this is applicable to you...

-The Bearer-

QUOTE (The Bearer @ Sep 9 2008, 12:04 PM)

QUOTE (Brouk @ Sep 9 2008, 05:51 AM)

70°C clear water for 1 min, if this is applicable to you...

For what application did you use this approach?

-Brouk-

QUOTE (Brouk @ Sep 10 2008, 02:09 AM)

QUOTE (The Bearer @ Sep 9 2008, 12:04 PM)

QUOTE (Brouk @ Sep 9 2008, 05:51 AM)

70°C clear water for 1 min, if this is applicable to you...

For what application did you use this approach?

to recover streptavidin-coated microplates from bound biotin...it works

-The Bearer-

For streptavidin columns the supplier recommends 8 M guanidine-HCl, pH 1.5 as elution buffer
but the harsh conditions may affect your molecules.

Other way could be including free biotin in buffer for elution, may be it is able to
dissociate your biotin-tagged target from streptavidin.

-celvas-