"These materials separate proteins on the basis of hydrophobic character, as does Reversed-Phase Chromatography. HIC uses totally aqueous buffers, maintaining tertiary structure and biological activity. Typically, a sample is eluted with a decreasing gradient of a salt such as sulfate or phosphate. Proteins elute in order of increasing surface hydrophobicity. Surfactants (e.g. CHAPS, octylglucoside) can be added to the mobile phase if necessary. The relative hydrophobic character of PolyETHYL A is 60. When To Use HIC:
Characterization of antibodies.
Purification of polypeptides such as glycopeptides and venoms.
Isolation of proteins from crude extracts.
Quality control assay using a method complementary to ion-exchange and Reversed-Phase.
Isolation of integral membrane proteins and their complexes.
"
"These materials separate proteins on the basis of hydrophobic character, as does Reversed-Phase Chromatography. HIC uses totally aqueous buffers, maintaining tertiary structure and biological activity. Typically, a sample is eluted with a decreasing gradient of a salt such as sulfate or phosphate. Proteins elute in order of increasing surface hydrophobicity. Surfactants (e.g. CHAPS, octylglucoside) can be added to the mobile phase if necessary. The relative hydrophobic character of PolyETHYL A is 60.
When To Use HIC:
- Characterization of antibodies.
- Purification of polypeptides such as glycopeptides and venoms.
- Isolation of proteins from crude extracts.
- Quality control assay using a method complementary to ion-exchange and Reversed-Phase.
- Isolation of integral membrane proteins and their complexes.
"
