Two-dimensional gel electrophoresis
Two-dimensional gel electrophoresis (pronunciation: two-di-men-shuh-nl jel ih-lek-troh-fer-uh-sis) is a technique in biochemistry for separating proteins based on two distinct properties: their isoelectric point and their molecular weight. The method was first introduced by O'Farrell, P.H. in 1975.
Etymology
The term "Two-dimensional gel electrophoresis" is derived from the process itself. "Two-dimensional" refers to the two distinct properties (isoelectric point and molecular weight) used for protein separation. "Gel" refers to the medium (usually polyacrylamide or agarose) used for the electrophoresis. "Electrophoresis" is a term derived from the Greek words "electron" (amber), referring to electricity, and "phoresis" (to carry), referring to the movement of particles under the influence of an electric field.
Procedure
The procedure of two-dimensional gel electrophoresis involves two steps. The first dimension is isoelectric focusing (IEF), where proteins are separated based on their isoelectric point (pI). The second dimension is SDS-PAGE, where proteins are further separated based on their molecular weight.
Related Terms
- Isoelectric focusing (IEF): A technique used to separate proteins based on their isoelectric point.
- SDS-PAGE: A method used to separate proteins based on their molecular weight.
- Proteomics: The large-scale study of proteins, particularly their structures and functions.
- Polyacrylamide gel: A type of gel used in electrophoresis.
- Agarose gel: Another type of gel used in electrophoresis.
See Also
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