Streptavidin from Streptomyces avidinii

Streptavidin derives its name from its bacterial source Streptomyces avidinii and from the hen egg-white protein, avidin, which has high affinity to biotin. Its homologous core shares 33% sequence similarity with avidin, as well as sharing a common tetrameric structure. It is a crystalline tetrameric protein, with a molecular weight of 4*15000Da. It binds four molecules of biotin. Streptavidin lacks carbohydrate and sulfur-containing amino acids.

Streptavidin is a crystalline protein isolated from the bacterium Streptomyces avidinii and possesses biotin-binding ability. It has four binding sites for biotin like avidin and binds four molecules of biotin. Streptavidin is now considered as a new type of biotin-binding protein.

Streptavidin from Streptomyces avidinii has been used:

• in wire functionalization
• in streptavidin capture enzyme-linked immunosorbent assay (ELISA)
• in microbubble preparation

Affinity purified.

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