BMSC 240 Laboratory Techniques Lecture 14: Chromatography

Flashcards covering key concepts and vocabulary from Lecture 14 on Chromatography techniques.

Chromatography

Techniques to separate mixtures based on physical properties such as size or charge.

Stationary phase

A substance that the compounds to be separated pass by or interact with.

Mobile phase

The carrier for the compounds to be separated.

Differential Precipitation

A method to make some proteins less soluble by altering the temperature, salinity, or pH.

Salting Out

A common & reversible method where increased salt concentration causes proteins to aggregate and lose solubility.

Dialysis

A method to remove excess salt by allowing smaller molecules to pass through pores in dialysis tubing.

Size Exclusion Chromatography

A method where proteins are separated based on their size, with larger proteins eluting first.

Partition Coefficient (Kav)

The fraction of the pores within the beads available to the sample, used to estimate molecular weight.

Ion Exchange Chromatography

A method where charged beads form the stationary phase, separating proteins based on their charge.

Affinity Chromatography

A technique that captures a specific protein of interest through interaction with a ligand attached to the stationary phase.

SDS-PAGE

Sodium dodecyl sulfate polyacrylamide gel electrophoresis, a method to denature proteins and separate them based on size.

Electrophoresis

A method that involves the migration of ions in an electric field, with velocity dependent on charge and size.

order of specificity

affinity, ion exchange, size exclusion

Protein Gel Electrophoresis

A technique used to separate proteins based on their size and charge through a gel matrix, allowing for analysis and identification.