Purification of Lipase and Other Lipolytic Enzymes from the Human Pancreas

Abstract

A pure lipase has been isolated from extracts of the human pancreas. The purification process includes centrifugation, two ion-exchange chromatography steps, and one gel filtration step. Compared with other reports, a high recovery, large amounts, and a high specific activity were obtained. Lipase is present at 1–2 mg/g in the pancreatic gland. In the absence of colipase and bile salts with tributyrine as substrate, the specific activity at room temperature and at pH 7.0 is 4000 μmol/min/mg. It increases to 8000–10,000 in the presence of colipase and bile salts at a temperature of 37°C. The fate of the other human lipolytic proteins during the different purification steps is also indicated. Lipase purified by this method has been used for crystallization.

Key Words:

• Carboxyl ester lipase
• colipase
• human
• lipase
• pancreas
• phospholipase A₂
• purification