Biochemistry - Ch 05 - Lecture 6, 7 - Protein Purification (Vocab)

Front 1

Define:

Affinity Chromatography

Back 1

A procedure in which a molecule is separated from a mixture of other molecules by its ability to bind specifically to an immobilized ligand.

See also metal chelate affinity chromatography

Front 2

Define:

Anion Exchanger

Back 2

A cationic matrix used to bind anionic molecules in ion exchange chromatography

Front 3

Define:

Assay

Back 3

A laboratory technique for detecting, and in many cases quantifying, a macromolecule or its activity.

Front 4

Define:

Chromatography

Back 4

A technique for separating the components of a mixture of molecules based on their partition between a mobile solvent phase and a porous matrix (stationary phase).

Front 5

Define:

Coupled Enzymatic Reaction

Back 5

A technique in which the activity of an enzyme is measure by the ability of a second enzyme to use the product of the first enzymatic reaction to produce a detectable product.

Front 6

Define:

Denature

Back 6

To disrupt the native conformation of a polymer.

Front 7

Define:

Edman Degradation

Back 7

A procedure for the stepwise removal and identification of the N-terminal residues of a polypeptide.

Front 8

Define:

ELISA

Back 8

Enzyme-linked immunosorbent assay (ELISA)

A technique in which a molecule is detected, and in many cases quantified, by its ability to bind an antibody to which an enzyme with an easily detected reaction product is attached.

Front 9

Define:

Fractionation procedure

Back 9

A laboratory technique for separating the components of a mixture of molecules through differences in their chemical and physical properties.

Front 10

Define:

Gel Filtration Chromatography

Back 10

A procedure in which macromolecules are separated on the basis of their size and shape.

Also called 'size exclusion' or 'molecular sieve' chromatography.

Front 11

Define:

Hydrophobic Interaction Chromatography

Back 11

A procedure in which molecules are selectively retained on a nonpolar matrix by virtue of their hydrophobicity.

Front 12

Define:

Immunoassay

Back 12

A procedure for detecting, and in some cases quantifying the activity of, a macromolecule by using an antibody or mixture of antibodies that reacts specifically with that substance.

Front 13

Define:

Ion Exchange Chromatography

Back 13

A fractionation procedure in which ions are selectively retained by a matrix bearing oppositely charged groups.

Front 14

Define:

Ligand

Back 14

(1) A small molecule that binds to a larger molecule.

(2) A molecule or ion bound to a metal ion.

Front 15

Define:

Mass Spectrometry

Back 15

A technique for identifying molecules by measuring the mass-to-charge ratios of molecular ions in the gas phase.

Front 16

Define:

Multisubunit Protein

Back 16

A protein consisting of more than one polypeptide chain (subunit)

Front 17

Define:

Nuclease

Back 17

An enzyme that hydrolytically degrades nucleic acids.

Front 18

Define:

PAGE

Back 18

Polyacrylamide gel electrophoresis.

See gel electrophoresis

Front 19

Define:

Peptide

Back 19

A polypeptide of less than about 40 residues.

Front 20

Define:

Primary Structure

Back 20

The sequence of residues in a polymer.

Front 21

Define:

Protease

Back 21

(a.k.a. peptidase)

An enzyme that hydrolyzes peptide bonds.

Also called a protease.

Front 22

Define:

Salting In

Back 22

The increase in solubility of a protein (or other molecule) with increasing (low) salt concentration.

Front 23

Define:

Salting Out

Back 23

The decrease in solubility of a protein (or other molecule) with increasing (high) salt concentration.

Front 24

Define:

SDS-PAGE

Back 24

Polyacrylamide gel electrophoresis (PAGE) in the presence of the detergent sodium dodecyl sulfate (SDS), which denatures and imparts a uniform charge density to polypeptides and thereby permits them to be fractionated on the basis of size rather than inherent charge.

Front 25

Define:

Subunit

Back 25

One of several polymer chains that make up a macromolecule.