Capillary electrophoresis (CE) - separation analysis method
CE was invented by Hjerten in the late 1960s based on traditional electrophoresis technology. It uses small capillaries instead of traditional large electrophoresis tanks to increase the electrophoresis efficiency by several tens of times. This technology has developed rapidly since the 1980s and is a useful tool for biochemical analysts and biochemists to separate and characterize antigenic peptides and proteinaceous materials. CE can be divided into the following according to the application principle; Capillary Zone electrophoresis (CZE), Capillary Isoeletric Focusing (CIEF) Capillary Gel Electrophoresis (CGE) and micellar electrocapillary layer Analysis (Micellar Electokinetic Electrophoresis Chromatorgraphy, MECC) and the like.
1 Capillary Zone Electrophoresis (CZE)
CZE separation of peptides is mainly determined by the chargeability of compounds in different components, which is more accurate than traditional gel electrophoresis. The main problem currently existing in CZE separation and analysis of peptide materials is that natural proteins or peptides easily react with silanol on the capillary silica gel column, affecting peak shape and electrophoresis time. Many scholars have done a lot of experiments to improve these problems, such as adjustment. The pH of the battery bath reduces the polar groups reactive with silanol; improves the composition of the capillary column material, and uses different CZE methods to separate 5 small peptides containing 9 amino acid residues for different antigen peptide properties. The basic conditions for the analysis of small peptides were determined, that is, under low pH conditions, the buffer contained a certain concentration of metal ions such as Zn2+, and the separation speed was fast and accurate.
2 Capillary Isleletric Focusing (CIEF)
Due to the different isoelectric points (PI) of different proteins and polypeptides, in an electrophoresis tank with different pH gradients, it can be aggregated and precipitated at isoelectric point pH, and separated from other peptides. CIEF is not widely used in the separation and analysis of mixed antigen peptide materials. It mainly uses separation between polypeptide isomers from different sources, such as separation of different isomers of rHG. The wide application of this method is limited by the instability of the surface covering on the CIEF column.
3 Capillary Gel Electrophoresis (CGE)
CGE is based on the molecular sieve principle. Proteins or peptides treated with sodium dodecyl sulfate (SDS) are mainly separated by molecular shape and molecular weight during electrophoresis. At present, there is a non-cross-linked, linear, hydrophobic poly-gel column for the separation and analysis of peptide substances. This electrophoresis method is suitable for peptide separation with more hydrophobic side chains. This gel is easy to perfuse and has a service life. Long, the nature is relatively stable.
4 Micellar Electrokinetic Electorphoresis Chromatography (MECC)
The principle of MECC is to add a surfactant, such as SDS, to the electrophoresis fluid to separate some neutral molecules with the same charge molecules. Especially for the application of some small molecular peptides, anionic and cationic surfactants, it can form a micelle with a certain charge, so as to obtain a good separation effect. Http:// It has been reported in the literature that cyclodextrin and other substances are added to the electrolyte, and the selectivity of the polypeptide containing the hydrophobic structural component and the ring hole of the cyclodextrin can be used to utilize the hydrophobic action. The polypeptide is isolated.
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