FDSC 305 Study Guide - Midterm Guide: Ammonium Sulfate, Ionic Strength, Sodium Chloride

124 views4 pages

Document Summary

Separation using hic is based on the reversible interaction between a protein and the hydrophobic ligand bound to the chromatography matrix. Hydrophobic amino acids of proteins and peptides are usually located away from molecular surfaces. However, many biomolecules have some hydrophobic groups that are sufficiently exposed to allow interaction with hydrophobic ligands on media. Compared to reversed phase chromatography, the density of the ligand on the matrix is much lower and allows mild elution conditions, helping to preserve biological activity. Hic is particularly suitable for samples precipitated with ammonium sulfate or eluted in high salt concentrations since high ionic strength buffers enhance the hydrophobic interaction. The interaction is enhanced by buffers with high ionic strength, which makes hic an excellent purification step after ammonium sulfate precipitation or after elution in high salt during ion exchange chromatography (iex). Hic is well- suited for the capture or intermediate steps in a purification scheme.

Get access

Grade+20% off
$8 USD/m$10 USD/m
Billed $96 USD annually
Grade+
Homework Help
Study Guides
Textbook Solutions
Class Notes
Textbook Notes
Booster Class
40 Verified Answers