Abstract
Streptavidin, a protein produced by Streptomyces avidinii, binds a water-soluble vitamin, D-biotin (vitamin H), with remarkably high affinity (1,2). The dissociation constant of the streptavidin-biotin complex is approx 10−15 M; the binding of streptavidin to biotin is one of the strongest noncovalent interactions found in biological systems. The extremely tight and specific biotin-binding ability of streptavidin has made this protein a very powerful biological tool for a variety of biological and biomedical analyses (3,4). The ability of biotin to be incorporated easily into various biological materials has also expanded the application of the streptavidin-biotin technology to a wider range of biological systems.
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© 1997 Humana Press Inc., Totowa, NJ
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Sano, T., Smith, C.L., Cantor, C.R. (1997). Expression and Purification of Recombinant Streptavidin-Containing Chimeric Proteins. In: Tuan, R.S. (eds) Recombinant Protein Protocols. Methods in Molecular Biology™, vol 63. Humana Press. https://doi.org/10.1385/0-89603-481-X:119
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DOI: https://doi.org/10.1385/0-89603-481-X:119
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