ion-exchange chromatography


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ion-exchange chromatography

[′ī‚än iks‚chānj ‚krō·mə′täg·rə·fē]
(analytical chemistry)
A chromatographic procedure in which the stationary phase consists of ion-exchange resins which may be acidic or basic.
References in periodicals archive ?
Crude enzyme sample showed a number of smeared bands while three bands and one band was obtained after gel filtration and single band after ion-exchange chromatography, respectively (Figure-4).
Selection of a suitable mobile phase for the speciation of four arsenic compounds in drinking water samples using ion-exchange chromatography coupled to inductively-coupled plasma-mass spectrometry.
Similarly, anion ion-exchange chromatography may also be utilized for the purification of the two hemocyanin subunit types in oligomeric state but with relatively lesser reproducibility (Swerdlow et al., 1996; Gebauer et al., 1999; Schutz et al., 2001).
Purification stages Chromatographic Yield Specific fraction (mg) hemolytic activity (HU/mg) Extraction - 1700 212 Ion-exchange chromatography on Q1 543 572 Q-Sepharose Ion-exchange chromatography on SP1 178 1620 SP-Sepharose Hydrophobic interaction PS2 62 4510 chromatography on Phenyl-Sepharose Gel filtration on Superdex 75 S3 16 13.650 Purification stages Total hemolytic Recovery activity (HU) of HU (%) Extraction 360,400 Ion-exchange chromatography on Q-Sepharose 310,600 87 Ion-exchange chromatography on 288,400 80 SP-Sepharose Hydrophobic interaction chromatography on 279,600 76 Phenyl-Sepharose Gel filtration on Superdex 75 218,400 61 HU: hemolytic unit.
These researchers fed rats food containing 15 [micro]g/g Se as selenite with added [sup.75]Se selenite; they also used ion-exchange chromatography and reineckate salt precipitation to isolate the compound.
They're using ion-exchange chromatography to purify the proteins from whey.
Ion-exchange chromatography is one of the most popular methods for biological substances, in part because researchers can separate biomolecules that differ in charge only a little.
Lactate dehydrogenase is purified from the heart ventricles of river buffalo by ion-exchange chromatography followed by the removal of some unwanted proteins by selective ammonium sulfate precipitations.
The two most common principles include those based on charge differences (ion-exchange chromatography and electrophoresis), and structural differences (boronate-affinity chromatography and immunoassay) of HbA1c.