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Can a biotin:streptavidin complex be disrupted?
The biotin:streptavidin interaction, with a Kd of
10-15M, is one of the strongest and most stable interactions known in biology.
Streptavidin exists as a 66kDa tetramer capable of binding four molecules of biotin. It is
this tetrameric structure that is responsible for the high affinity of streptavidin for
biotin. In addition, the streptavidin tetramer is remarkably stable; it remains intact in
urea up to 7M and its unfolding is sluggish in guanidine hydrochloride at 6M. However, the
interaction between streptavidin and a biotinylated oligo can be disrupted by heating the
complex in a buffer containing 2M beta-mercaptoethanol (1).
Reference
- Jenne, A. and Famulok, M. (1999) Disruption of the streptavidin interaction with
biotinylated nucleic acid probes by
2-mercaptoethanol. BioTechniques 26, 249.
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