Protein Chemistry: Structure, Properties, and Research Methods - Shendryk, A.N. 2022

Methods for Experimental Study of Protein Structure
Protein Separation Methods
Electrophoresis

In 1809, Prof. O.Yu. Reuss of Moscow University was the first to describe the principles governing the movement of charged particles in colloidal solutions within an electric field, thereby laying the foundations of modern electrophoresis (EP). Today, electrophoresis (formerly known as cataphoresis) is widely used to study colloidal systems and protein solutions. The migration of low-molecular-weight electrolyte ions in an electric field is referred to as ionophoresis.

Electrophoresis is classified into preparative and analytical types. Preparative EP is used to isolate relatively large quantities of material, whereas analytical EP serves research purposes such as purity control and mixture composition analysis.

In addition, EP is categorized by scale into macroelectrophoresis (Separation of more than 100 mg of a substance), microelectrophoresis (separation of less than 1 mg of a substance), and semimicroelectrophoresis (separation of 1–10 mg of a substance), as well as by voltage into low-voltage (up to 1000 V) and high-voltage (exceeding 1000 V).

Electrophoresis can be used to separate Proteins, Nucleic Acids, Polysaccharides, Enzymes, toxins, phosphate esters, bacterial Antigens, Viruses, Vitamins, Antibiotics, Alkaloids, and a variety of other substances.

In modern practical Analytical Methods based on electrophoresis, the movement of substances takes place in a liquid buffer medium held by an inert solid support, such as paper or gels. The liquid medium acts as a conductor within the externally applied electric field.



Last update: 06/08/2026

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