Affinity electrophoresis

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In biochemistry, affinity electrophoresis includes all electrophoretic processes in which a modified flow behavior of molecules (e.g. protein complexes or DNA- protein complexes) is generated by the affinity of two or more molecules to one another. Due to the changed running speeds, affinity electrophoretic methods are also known as electrophoretic shift assays .

Procedure

Depending on the observed parameters of an electrophoresis, the applications are referred to as mobility shift electrophoresis (with tracked tracking), charge shift electrophoresis (with tracked isoelectric point ) or affinity capillary electrophoresis (with capillary electrophoresis ).

Affinity electrophoretic methods for the detection of protein-protein interactions are e.g. B. QPNC-PAGE, Clear-Native-PAGE , Blue-Native-PAGE or SDS-PAGE after cross-linking .

The interaction of DNA with proteins can be detected by an electrophoretic mobility shift assay or a capillary electrophoresis.

A binding of carbohydrates to proteins (e.g. of polysaccharides to lectins ) can be investigated by lectin affinity electrophoresis .

literature

Individual evidence

  1. ^ NH Heegaard, RT Kennedy: Identification, quantitation, and characterization of biomolecules by capillary electrophoretic analysis of binding interactions . In: Electrophoresis . tape 20 , no. 15-16 , October 1999, pp. 3122-3133 , doi : 10.1002 / (SICI) 1522-2683 (19991001) 20: 15/16 <3122 :: AID-ELPS3122> 3.0.CO; 2-M , PMID 10596820 .
  2. Kazuaki Kakehi, Mitsuhiro Kinoshita: Capillary lectin-affinity electrophoresis for glycan analysis . In: Methods in molecular biology . tape 534 , 2009, pp. 93-105 , doi : 10.1007 / 978-1-59745-022-5_7 , PMID 19277533 .