Abstract
Biotin is an essential coenzyme, which displays its biological activity only when covalently bound to specific metabolic key enzymes. Examples of these enzymes, which are basically involved in carboxylation reactions, include pyruvate carboxylase, trans-carboxylase, acetyl-CoA-carboxylase, s-methylcrotonyl-CoA carboxylase and geranoyl-CoA carboxylase. There are several proteins known that bind biotin with extremely high affinity. Avidin from egg yolk and streptavidin from culture broth of Streptomyces avidinii are the most popular. With Kd values around 10-15 M-1, their binding to biotin is the strongest known non-covalent biological interaction. Based on this interaction, a plurality of methods for immobilization, purification and detection of proteins has been developed. Also a variety of avidin and streptavidin analogues or derivatives were made with impaired biotin-binding strength either by chemical modification, partial denaturation or genetical engineering. These weaker binders are expecially helpful in cases where a gentle isolation procedure of a protein is needed which does not harm its functionality.
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