Protein/enzyme inactivation during different chromatographic methods of separation.
Protein denaturations encountered during the different types of chromatographic separations are presented. The analysis of different protein denaturations presented along with the causes of such denaturations provides a judicious framework to compare protein denaturations encountered by such separation techniques. Especially of interest are those studies which compare the mass recovery of proteins and the retention of activity by different chromatographic techniques. Reversed-phase chromatography is presented even though it is utilized nowadays only for specialized cases such as separation of small peptides. It appears that relatively mild interactions that are encountered generally in hydrocarbon-interaction chromatography are favorable to the preservation of the native (active) protein state. The few available mechanistic studies presented provide judicious physical insights into protein conformational behavior on chromatographic columns.
Chemical Engineering Department, University of Mississippi, University 38677-9740.
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Sadana
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Raju
D000818:Animals; D002845:Chromatography / Q000379:methods*; D004798:Enzymes / Q000737:chemistry / Q000302:isolation & purification*; D006801:Humans; D011489:Protein Denaturation; D011506:Proteins / Q000737:chemistry / Q000302:isolation & purification*
D004798:Enzymes; D011506:Proteins