electrophoresis(redirected from Two-dimensional gel electrophoresis)
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the movement of charged particles suspended in a liquid on various media (e.g., paper, gel, liquid) under the influence of an applied electric field. adj., adj electrophoret´ic. 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 is therefore valuable in the study of diseases in which the serum and plasma proteins are altered. The principle also has been applied in the separation and identification of various types of human hemoglobin.
The movement of particles in an electric field toward an electric pole (anode or cathode); used to separate and purify biomolecules.
See also: electropherogram.
See also: electropherogram.
[electro- + G. phorēsis, a carrying]
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
counter electrophoresis counterimmunoelectrophoresis.
1. The migration of charged colloidal particles or molecules through a stationary medium under the influence of an applied electric field usually provided by immersed electrodes. Also called cataphoresis.
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.
e·lec′tro·pho·ret′ic (-rĕt′ĭk) adj.
Etymology: Gk, elektron + pherein, to bear
the movement of charged suspended particles through a liquid medium in response to changes in an electric field. Charged particles of a given substance migrate in a predictable direction and at a characteristic speed. The pattern of migration can be recorded in bands on an electrophoretogram. The technique is widely used to separate and identify serum proteins and other substances. electrophoretic, adj.
electrophoresisLab methods A method of separating large molecules–eg, DNA fragments or proteins from a mixture of similar molecules, by passing an electric current through a medium containing the mixture; each molecule travels through the medium at a different rate, depending on its electrical charge and size; agarose and acrylamide gels are media commonly used electrophoretic media
electrophoresisSeparation of charged particles in a solution (ions) by the application of an electric current. This can be done in a thin layer of solution on paper or in a gel. Ions of low weight move more quickly than those of high weight, so separation occurs and can be demonstrated by staining. The method is widely used in medicine to identify and measure the proteins present in the blood including the ANTIBODIES (IMMUNOGLOBULINS). It is used to identify the various abnormal haemoglobins causing SICKLE CELL ANAEMIA and other similar conditions. It is extensively used in genetic work such as DNA fingerprinting. Electrophoresis is remarkably sensitive. Pieces of DNA, for instance, that differ in length from each other by only one base pair can be separated into discrete bands by this method.
electrophoresisa method for separating particles with different electrical charges, for example, amino acids, peptides, proteins and nucleic acids. The apparatus consists of a supporting medium soaked in a suitable buffer with an electrical field set up across it. The mixture to be separated (e.g. blood proteins) is placed on the supporting medium. The components with different charges then separate from each other and their eventual position is compared with the position of known standards.
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.
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.
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.
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.