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==Use in biotechnology==
Chemically modified versions of biotin are widely used throughout the [[biotechnology]] industry to isolate proteins and non-protein compounds for biochemical [[assay]]s. Because egg-derived [[avidin]] binds strongly to biotin with a [[dissociation constant]] ''K''<sub>d</sub> ≈ 10<sup>−15</sup> M, biotinylated compounds of interest can be isolated from a sample by exploiting this highly stable interaction. First, the chemically modified biotin reagents are bound to the targeted compounds in a solution via a process called biotinylation. The choice of which chemical modification to use is responsible for the biotin reagent binding to a specific protein. Second, the sample is incubated with avidin bound to beads, then rinsed, removing all unbound proteins, while leaving only the biotinylated protein bound to avidin. Last, the biotinylated protein can be eluted from the beads with excess free biotin. The process can also utilize bacteria-derived [[streptavidin]] bound to beads, but because it has a higher dissociation constant than avidin, very harsh conditions are needed to elute the biotinylated protein from the beads, which often will denature the protein of interest.

Translations:Biotin/29/en - Revision history

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