No abstract

No abstract

No abstract

The cell-free supernatant from homogenized bovine aorta hydrolyzed triglycerides, β-naphthylesters of lauric and stearic acid and Tween 20, 40 and 60. The rate of hydrolysis decreases as the acyl chain length of the substrates increases. The activity against triglycerides of short-chain fatty acids and monoacylesters could be partially separated from that of glycerol-trioleate lipase by ammonium sulfate fractionation. The activity of glycerol-trioleate lipase remained unaffected by heating for 5 min at 60 °C or by addition of bile acids, whereas the activity causing hydrolysis of triglycerides with short-chain fatty acids and monoacylesters decreases up to 60% by analogous treatment. No changes in the hydrolytic activity occurs in presence of sodium heparin. This indicates that this activity is not identical with a lipoprotein lipase.