Ion Exchange Chromatography

g A. Ion trade Chromatography Ion exchange chromatography is a process for separating proteins and other breakwaterecules in a solution based on differences in net charge. Ion Exchange Chromatography relies on charge-charge interactions between the proteins in your sample and the charges immobilized on the resin of your choice.Ion exchange chromatography can be subdivided into cation exchange chromatography, in which positively aerated ions bind to a negatively aerated resin and anion exchange chromatography, in which the salad dressing ions be negative, and the immobilized functional group is positive. formerly the solutes are bound, the column is washed to poise it in your starting fan, which should be of low-spirited ionic strength, and then the bound molecules are eluted off utilise a gradient of a second buffer which steadily increases the ionic strength of the eluent solution.Alternatively, the pH of the eluent buffer can be modified as to give your protein or the ma trix a charge at which they will non interact and your molecule of interest elutes from the resin. In the study of LU Rong-Rong, et al. lactoferrin was extracted from bovine colostrums using ion exchange chromatography by SP Sepharose Fast prevail (SP Sepharose FF) of excellent absorption specialty for LF, was elect as the ion exchange with elution rate of 2 L/h. 0. mol/L NaCl aqueous solution was used to elute the secretory immunoglobulin A and lactoperoxidase. Then, lactoferrin was eluted with 1. 0 mol/L NaCl aqueous buffer. Lactoferrin fraction is shown as a single band in SDS-PAGE with molecular weight of 80400 Da. The isoelectric point of lactoferrin is 8. 65 determined by isoelectric focusing. The purity of full-strength LF on pilot production is 94. 20% with a yield of 75. 45%. point of reference Retrieve from http//124. 205. 222. 100/Jwk_spkx/EN/ nonobjective/abstract14803. shtml