What is hydrophobic interaction chromatography?
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Hydrophobic interaction chromatography (HIC) isolates particles dependent on their hydrophobicity. HIC is a helpful division procedure for cleansing proteins while keeping up organic action because of the utilization of conditions and grids that work under less denaturing conditions.
This segment gives a review of hydrophobic connection chromatography with general contemplations about different factors, for example, the ligand, framework, salt fixation, pH, and temperature.
This segment gives a review of hydrophobic connection chromatography with general contemplations about different factors, for example, the ligand, framework, salt fixation, pH, and temperature.
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--> Hydrophobic Interaction Chromatography technique is used to differentiate proteins on the basis of hydrophobocity from one another.
--> Usually Aluminium Sulfate is used as a buffer in this type of chromatography because of its high ionic strength.
--> Stationary Column is attached with hydrophobic groups such as phenyl, octyl and butyl.
--> The hydrophobic groups bind with the hydrophobic amino acid side chains of the proteins which pass through the Stationary Column.
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