Studies on Lipase.

Lipase from different tissues was extracted in potassium phosphate buffer containing sodium deoxycholate and purified by column chromatography on Sephadex and Sepharose gels. A 500fold purification was achieved by this procedure. This purified enzyme has an estimated molecular weight greater than 3 × 106, and it runs as a single protein band in polyacrylamide preparative disc gel electrophoresis. After acetone — ether treatment of the etude rat pancreactic lipase extract. the resulting enzyme has an estimated molecular weight less than 3 × 104, similar to those reported in the literature. The purified enzyme catalyzes the hydrolysis of long and short chain fatty acid glycerol esters. Phenoxybenzamine and phentolamine were found to inhibit the hydrolysis of the long chain fatty acid glycerol esters by the high molecular weight lipase, while that by the low molecular weight lipase was not inhibited. When administered to rats in vivo, phenoxybenzaamine and phentolamine inhibited the hydrolysis of tripalmitin by the epididymal fat lipase: but the pancreatic or intestinal lipase activity was not affected. [ABSTRACT FROM AUTHOR]