Electrophoresis

electrophoresis /elec·tro·pho·re·sis/ (e-lek?tro-fah-re´sis) the separation of ionic solutes based on differences in their rates of migration in an applied electric field. Support media include paper, starch, agarose gel, cellulose acetate, and polyacrylamide gel, and techniques include zone, disc (discontinuous), two-dimensional, and pulsed-field.electrophoret´ic

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counter electrophoresis  counterimmunoelectrophoresis.

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e·lec·tro·pho·re·sis (-lktr-f-rss)

n.

1. The migration of charged colloidal particles or molecules through a solution under the influence of an applied electric field usually provided by immersed electrodes. Also called ionophoresis, phoresis.

2. A method of separating substances, especially proteins, and analyzing molecular structure based on the rate of movement of each component in a colloidal suspension while under the influence of an electric field.

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e·lectro·pho·retic (-rtk) adj.

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Electrophoresis

Use of an electrical field to separate proteins in a mixture (such as blood or urine), on the basis of the size and electrical charge of the proteins.

Mentioned in: AIDS Tests, Multiple Myeloma, Protein Electrophoresis

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electrophoresis (i·lekˈ·trō·f·rēˑ·sis),

n method used to separate particles, such as DNA or proteins, in which an electric current is passed through the medium and the separation of the molecules depends on the rate at which they travel towards the electrode based on their electrical charge.

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electrophoresis,

n the movement of charged suspended particles through a liquid medium in response to changes in an electric field.

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electrophoresis

the movement of charged particles suspended in a liquid through various media, e.g. paper, cellulose acetate, gel, liquid, under the influence of an applied electric field.

The various charged particles of a particular substance migrate in a definite and characteristic direction—toward either the anode or the cathode—and at a characteristic speed. This principle has been widely used in the separation of proteins and nucleic acids and is therefore valuable in the study of diseases in which the serum and plasma proteins are altered. See also immunoelectrophoresis.

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SDS-polyacrylamide gel electrophoresis (SDS-PAGE)

a procedure that revolutionized the analysis of complex mixtures of proteins. The proteins are solubilized by the powerful, negatively charged detergent sodium dodecyl sulfate (SDS) which causes proteins to unfold into extended, single polypeptide chains. A reducing agent such as mercaptoethanol is usually added to break disulfide bonds. The constituent polypeptides are then electrophoresed through an inert matrix of highly cross-linked gel of polyacrylamide. The pore size of the gel can be varied by altering the concentration of polyacrylamide.

two-dimensional gel electrophoresis

a SDS-polyacrylamide gel electrophoresis run, first in one direction, then again at right angles. In the first dimension an isoelectric-focusing gel is run and in the second dimension the proteins are separated in SDS-PAGE. A greater number of individually different proteins can be resolved in a highly repeatable fingerprint-like pattern.