BMSC 240 Laboratory Techniques Lecture 16: Protein Electrophoresis

These flashcards cover key terminology and concepts from the lecture on Protein Electrophoresis, including techniques, methods, and biological processes relevant to the field.

Protein Electrophoresis

A technique used to separate proteins based on size, charge, and conformation under an electric field.

SDS (Sodium Dodecyl Sulfate)

A detergent used to denature proteins and provide them with a negative charge for electrophoresis.

Denaturation

The process of breaking down the structure of proteins, often achieved through heat, chemicals, or pressure.

Isoelectric Point (pI)

The pH at which a protein has no net charge.

Ampholytes

Molecules that help maintain a stable pH gradient in gels during isoelectric focusing.

Native Gel

A type of gel where proteins are not denatured and retain their functional forms.

Coomassie Staining

A common staining method used to visualize proteins in gels.

2-Dimensional Gel Electrophoresis

A technique that separates proteins based on two different properties (usually size and charge) in two dimensions.

Urea Denaturing Gels

Gels that include urea to denature proteins while retaining their charge properties.

Staining Sensitivity

The amount of protein required for detection using different staining methods.

Clonal Selection (B-cell Activation)

The process by which B-cells proliferate and differentiate into plasma or memory cells upon exposure to their specific antigen.

Antibodies

Proteins produced by B-cells that specifically bind to antigens to neutralize pathogens.

IgG (main),IgM (first),IgA (secreted),IgD (dispensible),IgE (allergies)