Purification of hormone-sensitive lipase by high-performance ion exchange chromatography

We have developed an improved method for purification of hormone-sensitive lipase from adipose tissue. The method employs two preparative high-performance ion-exchange chromatography steps on Mono Q and Mono S after detergent solubilization and partial fractionation of the enzyme by gradient sievorptive chromatography on QAE-Sephadex. About 0.2 mg of greater than 70% pure enzyme is prepared at 10% yield within 6-7 days from adipose tissue of 500 rats. This protocol is a major improvement over the previously established procedure in terms of accessibility, rapidity, enzyme purity, and yield.