Interest of Using a Purified, Stable and Commutable Preparation of Human Pancreatic Lipase in Indirect Assays

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Abstract
Human lipase has been purified from pancreatic juice. The procedure involved ammonium sulphate fractionation, anion exchange chromatography, preparative isoelectric focusing, gel filtration and cation exchange chromatography. Apparent molecular weight and pI were found to be 48 kDa and 7.5 respectively. Purified enzyme supplemented with buffered human albumin 40 g/1 and sodium azide 1 g/1 was stable in solution at 4°C for at least 200 days. The effects of bile salts, colipase and ionic strength on enzyme activity were found to be very similar regardless of the source of the enzyme (pancreatic juice or plasma of patients suffering from acute pancreatitis). Studies of commutability indicated that the purified enzyme preparation described may provide a suitable calibrator for lipase indirect assays.