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Ion chromatography (or ion-exchange chromatography) is a form of chromatography that separates ions and ionizable polar molecules based on their affinity to the ion exchanger. [1] It works on almost any kind of charged molecule —including small inorganic anions, [ 2 ] large proteins , [ 3 ] small nucleotides , [ 4 ] and amino acids .
Atmospheric pressure chemical ionization chamber cross section. Atmospheric pressure chemical ionization (APCI) is an ionization method used in mass spectrometry which utilizes gas-phase ion-molecule reactions at atmospheric pressure (10 5 Pa), [1] [2] commonly coupled with high-performance liquid chromatography (HPLC). [3]
Schematic structure of DEAE-C: positively charged diethylaminoethanol groups can bind negative ions. Diethylaminoethyl cellulose (DEAE-C) is a positively charged resin used in ion-exchange chromatography, a type of column chromatography, for the separation and purification of proteins and nucleic acids.
ion exchange on DEAE Sepharose is run to bind the albumin to the column, Albumin is eluted with a sodium acetate buffer, and; Final polishing with gel filtration. The end result is a highly pure and safe batch of albumin that is 100% non-pyrogenic, sterile, and free of active HIV virus. The product purity is greater than 98% and the protein ...
Chromatofocusing is a powerful purification technique with respect to proteins as it can resolve very similar species differing by less than 0.05 pH units [2] that may not separate well, or at all, using traditional ion exchange strategies. A major drawback to this technique is that some proteins will aggregate when they are present at ...
Anion exchange resins will bind to negatively charged molecules, displacing the counter-ion. Anion exchange chromatography is commonly used to purify proteins, amino acids, sugars/carbohydrates and other acidic substances [3] with a negative charge at higher pH levels. The tightness of the binding between the substance and the resin is based on ...
In 1986, Regnier’s group synthesized a stationary phase that had characteristics of anion exchange chromatography (AEX) and hydrophobic interaction chromatography (HIC) on protein separation. [8] In 1998, a new form of MMC, hydrophobic charge induction chromatography (HCIC), was proposed by Burton and Harding.
Ion exchange chromatography is a very powerful tool for use in protein purification and is frequently used in both analytical and preparative separations. It is especially useful when purifying nucleic-acid binding proteins, where separation of the protein from the bound nucleic acid is required to obtain a pure sample devoid of nucleic acids ...
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