Membrane proteins may be identified by a shift in mobility induced by a charged detergent. The interaction or binding of a molecule, charged or uncharged, will normally change the electrophoretic properties of a molecule. The methods are based on changes in the electrophoretic pattern of molecules (mainly macromolecules) through biospecific interaction or complex formation. The methods include the so-called electrophoretic mobility shift assay, charge shift electrophoresis and affinity capillary electrophoresis. Both qualitative and quantitative information may be obtained through affinity electrophoresis. The analysis was performed early in the 1970s at the Protein LaboratoryĪffinity electrophoresis is a general name for many analytical methods used in biochemistry and biotechnology. Electrophoresis performed overnight at less than 10 V/cm. The quantitative principle of affinity electrophoresis illustrated with electrophoresis at pH 8.6 of concanavalin A into an agarose gel containing blood serum (3.6 microliter per square cm).
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