Anion exchange is a standard method for protein purification, yet it can be time-consuming and labor-intensive. Most purification regimes are performed at 4°C to minimize degradation and loss of activity, particularly important for thermolabile enzymes. We have developed a procedure for purifying a thermolabile, membrane-associated protein with a greater than 100-fold savings of time, greater purity and higher specific activity than can be achieved by conventional ion-exchange column chromatography.
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