Protein Purification and Enzyme Activity

Flashcards covering key concepts in protein purification and enzyme activity.

Chromatography

A technique based on varying degrees of component association between stationary and mobile phases.

Specific Activity

A measure of the purity of an enzyme.

Homogenization

The process of lysing cells and making their contents uniform.

Gel Filtration

A chromatography technique based on molecular size and weight.

Ion Exchange Chromatography

A chromatography method based on the net charge of amino acids/proteins at certain pH.

Edman Digestion

An efficient method that cleaves amino acids one at a time from the N-terminal of a peptide.

SDS-PAGE

Uses sodium dodecyl sulfate to denature proteins for separation based on size.

Michaelis-Menten Kinetics

Model describing enzyme kinetics in terms of substrate concentration affecting reaction rate.

Competitive Inhibition

Type of inhibition where the inhibitor increases Km without affecting Vmax.

Allosteric Enzymes

Enzymes that show cooperative kinetics and have a quaternary structure.

Feedback Inhibition

Process where the final product of a series of reactions inhibits the first step.

Affininty Chromatography

Separates proteins based on their specific interactions with a ligand attached to a resin.

Enzyme Activators

Substances that increase the activity of enzymes.

Proteolytic Enzymes

Enzymes that cleave peptide bonds to digest proteins into smaller fragments.

Cation Exchange

A chromatography method using negatively charged resin to exchange positive charges.

Anion Exchange

A chromatography method using positively charged resin to exchange negative charges.

Lineweaver-Burk Plot

A double reciprocal plot used to linearize Michaelis-Menten kinetics.

HPLC

High Pressure Liquid Chromatography, an effective and efficient method for separating compounds.

Enzyme Kinetics Equation

Expresses the relationship between reaction rate and substrate concentration.

Irreversible Inhibition

Inhibitor permanently binds to the enzyme, inactivating it.

Homotropic Effects

Effects due to binding of identical molecules to an enzyme.

Heterotropic Effects

Effects due to binding of different substances to an enzyme.