Protein Purification Techniques and Concepts

Environmental conditions such as X and X affect a protein’s stability during purification

• pH, temperature

• pH, solubility

• solubility, temparature

• charge, pH

An X based on a protein’s chemical or binding properties may be used to quantify a protein during
purification.

• fractionation

• assay

• preceptiation

• gel electrophoresis

Fractionation procedures take advantage of a protein’s unique structure and chemistry in order to
X it from other molecules

• precipitate

• quanitfy

• separate

• ultracentifugaration

Decreasing the salt concentration causes selective “salting out” (precipitation) of proteins with different
solubilities.

• True

• False

A protein’s ionic X ability influences its chromatographic behavior

• charge

• size

• polarity

• ligand binding

Can separate proteins according to charge, size, and isoelectric
point

• salting out

• fraction

• gel electrophoresis

separates based on the overall size and shape of macromolecules
and larger assemblies.

• Salting
  

• 
  Chromatography
  

• 
  • Gel electrophoresis
  

• 
  Ultracentrifugation

The purification procedure for ionic charge includes which of the following

• SDS Page

• Electrophoresis

• Affinity chromatography

• Ion exchange chromatography

In Ion Exchange Chromatography, positively charged proteins bind

• anion

• cation

Ion Exchange Chromatography, proteins are eluted (released) by
low salt concentration

• True

• False