PurificationStreptavdin was coupled to horseradish peroxidase using the periodate-method. The formed preparation is purified using column chromatography.
Streptavdin was coupled to horseradish peroxidase using the periodate-method.The formed preparation is purified using column chromatography. Streptavdin is a 53 kDa tetrameric protein composed of identic subunits. Each streptavidin subunit binds one biotin molecule with a high degree of affinity and specificity with KD of ~1x10-15 M which makes it one of the strongest known non-covalent interaction. Streptavidin is isolated from Streptomyces avidinii for use in isolation and detection bioassays.
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