Halophilic enzymes chromatography

Halophilic enzymes are very unstable in low salt concentrations. Because some of the important fractionation methods in protein chemistry, such as electrophoresis or ion-exchange chromatography, cannot be applied at high salt concentrations, the available fractionation methods are rather limited. This basic difficulty is the main reason why the number of halophilic enzymes studied in pure form is very small. 

A very interesting application of affinity chromatography to the purification of halophilic enzymes was reported by Sundquist and Fahey (1988). These authors have purified the enzymes bis-y-glu-tamylcysteine reductase and dihydrolipoamide dehydrogenase from H. halohium using immobilized metal ion affinity chromatography in high-salt buffers. 

Hydrophobic affinity chromatography in 119 the fractionation of enzymes from halophilic bacteria... 

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