Affinity chromatography: Difference between revisions
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Affinity [[Chromatography|chromatography]] separates [[Protein|proteins]] due to specific binding sites on the surface of the [[Protein|proteins]] that allow them to bind to particular small [[Molecule|molecules]] or macromolecules. The stationary phase will be an inert matrix that has the binding partner for the wanted [[Protein|protein]] attached to it. The separated [[Protein|protein]] can then be eluted using a [[Buffer|buffer]] which contains free binding partners for the [[Protein|protein]]. The eluted [[Protein|protein]] will be in a much purer form, often 1000 to 10,000 times more pure in a single pass <ref>Alberts B., Johnson A., Lewis J., Raff M., Roberts K and Walter P. (2002) Molecular Biology of the cell, 4th edition, New York: Garland and Science, Taylor and Francis group.</ref>.<br> | Affinity [[Chromatography|chromatography]] separates [[Protein|proteins]] due to specific binding sites on the surface of the [[Protein|proteins]] that allow them to bind to particular small [[Molecule|molecules]] or macromolecules. The stationary phase will be an inert matrix that has the binding partner for the wanted [[Protein|protein]] attached to it. The separated [[Protein|protein]] can then be eluted using a [[Buffer|buffer]] which contains free binding partners for the [[Protein|protein]]. The eluted [[Protein|protein]] will be in a much purer form, often 1000 to 10,000 times more pure in a single pass <ref>Alberts B., Johnson A., Lewis J., Raff M., Roberts K and Walter P. (2002) Molecular Biology of the cell, 4th edition, New York: Garland and Science, Taylor and Francis group.</ref>. This gives it an advantage over other methods of chromatography such as ion-exchange or gel chromoatography due to its products having higher purity. <br> | ||
=== References === | === References === | ||
<references /> | <references /> | ||
Revision as of 13:28, 21 October 2013
Affinity chromatography separates proteins due to specific binding sites on the surface of the proteins that allow them to bind to particular small molecules or macromolecules. The stationary phase will be an inert matrix that has the binding partner for the wanted protein attached to it. The separated protein can then be eluted using a buffer which contains free binding partners for the protein. The eluted protein will be in a much purer form, often 1000 to 10,000 times more pure in a single pass [1]. This gives it an advantage over other methods of chromatography such as ion-exchange or gel chromoatography due to its products having higher purity.
References
- ↑ Alberts B., Johnson A., Lewis J., Raff M., Roberts K and Walter P. (2002) Molecular Biology of the cell, 4th edition, New York: Garland and Science, Taylor and Francis group.