Hai friends, Sorry for the delay .The reason for the delay is because we were having exams. I am going to enhance your ideas which you have through my blog regarding "ION EXCHANGE CHROMTOGRAPHY".This is the widespread method which is used to separate proteins, charged particles especially.

Principle: The principle mainly involves interaction of ions in the sample with the oppositely charged ion groups on the exchanger. The process mainly involves 1. Making the ion exchanger ready for binding of solute molecules 2. Applying the sample after which the counter ions get replaced. 3. Removing the separated sample by changing making the elution techniques unsuitable for bonding. 4. Removing the left over substances which are not eluted. Ion exchanger is a matrix which has sites for binding of charged particals.There can be negatively charged exchangers for binding of positive counter ions and vice versa Nature of matrix: inorganic compounds, polysachrides, synthetic resins. Earlier cellulose exchangers were used because of its hydrophilic nature but it is replaces as it has poor flow properties. Later Dextran (Sephadex) and then agarose are being in use and even Sephacel (cross linked cellulose is used.(1) The strength of the exchanger depends upon the group present. Functional groups on Anion Exchangers: Diethylaminoethyl, Quarternary ammonium. Functional groups on cation Exchangers: Carbo methyl, sulphopropyl. The capacity of the exchanger has to be considered and this depends on * Protein properties * Ion exchanger properties * Experimental conditions Finally a small note on its application is this is used for purifying water and even for recovering metals like copper silver from waste waters and many more(2) Reference: (1)http://sbio.uct.ac.za/Sbio/documentation/Ion_exchange_chromatography.pdf dated 14th april 2011. (2) http://www.britannica.com/EBchecked/topic/292796/ion-exchange-reaction/4... dated 14th april 2011.