Abstract

An assay is described for the determination of very low levels of lipase activity, using as substrate an emulsion of radioactive triolein. By this method a triglyceride lipase activity (around 5 munitsJmg of protein) has been measured in crude extracts of human adipose tissue. The catalytic activity of this enzyme has been studied with respect to substrate concentration, pH, temperature and presence of various chemicals in the reaction mixture. Under the experimental conditions, enzymic hydrolysis was maximum at pH 7.5 and 40°. Reaction rates were increased in the presence of sodium taurocholate (10 mM), oleic acid (1 mM) and serum albumin (0.5%) in proportions of 380, 470 and 150%, respectively. Above the indicated concentrations, oleic acid and serum albumin became inhibitory.

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