Kinetic study of hepatic triglyceride lipase from rat liver soluble fraction.

An assay is described for the determination of lipase activity, using as substrate an emulsion of radioactive triolein with cholic acid as emulsifier. Lipase activity is given by determining radioactive triolein disappearance after incubation with the artificial emulsion. The catalytic activity of this enzyme has been studied with respect to time, protein concentration and substrate concentration. Under the experimental conditions, Michaelis constant value was 14.54 mmol/l and maximal hydrolysis rate 0.31 mumol h-1 mg-1.