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There are several advantages for using biotin-streptavidin/avidin (strept(avi-din)) systems to immobilize nucleic acids and other molecules. These include the essential irreversible, but not covalent, binding of biotin to strept(avidin), the ease of biotinylating a large number of molecules without interfering with their function or the binding of biotin by strept(avidin), and the stability of strept(avidin)...
The high affinity (k d =∼10 −15 M) of streptavidin and avidin for biotin is key to a large number of biological applications and is essentially irreversible unless the complex is exposed to harsh conditions (e.g. heat (100°C for 10min)), detergents, and/or denaturants which damage macromolecules. Thus, high binding affinity becomes a disadvantage when a biotinylated target must be...
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