2007
DOI: 10.1016/j.tibtech.2007.04.001
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Brave new (strept)avidins in biotechnology

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Cited by 177 publications
(144 citation statements)
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“…Due to the performance of these compounds, the absorption of water and electrolytes from the large intestine decreases and the volume and pressure of the intestinal contents increase. This condition stimulates the movement of the large intestine and prevents obstruction and excretion [32,33].…”
Section: Constipation Treatmentmentioning
confidence: 99%
“…Due to the performance of these compounds, the absorption of water and electrolytes from the large intestine decreases and the volume and pressure of the intestinal contents increase. This condition stimulates the movement of the large intestine and prevents obstruction and excretion [32,33].…”
Section: Constipation Treatmentmentioning
confidence: 99%
“…Because of their ability to bind biotin very tightly, they are widely used in (strept)avidinbiotin binding technology that is a common tool in life sciences and nanotechnology. To further improve these protein tools and obtain genetically engineered (strept)avidins, protein engineering methods were applied including simple amino acid substitutions to change physico-chemical properties, or more complex changes, such as chimeric (strept)avidins, topology rearrangements and non-natural amino acid stitching into the active sites (Laitinen et al, 2007).…”
Section: Protein Engineering 36mentioning
confidence: 99%
“…Among these, the covalent nature bonding affinity has advantageous over noncovalent bonding in the ability to orient the immobilized molecule in a defined and precise fashion for forthcoming reactions. The affinity of biotin for streptavidin is one of the strongest and most stable known in biochemistry [27]. Moreover, a wide range of immobilizing materials and binding modes allows a great deal of flexibility in order to design a specific bond with specific physical and chemical properties such as charge distribution, hydrophobic/hydrophilic, etc.…”
Section: Solid-phase Versus Solution-phase Chemistry For Protein Syntmentioning
confidence: 99%