Elevated phospholipase A 2 activities in serum were measured in patients suffering from acute pancreatitis or various inflammatory diseases. The photometric phospholipase A assay of Hoffmann & Neumann (Klin. Wochenschr. 67 (1989) 106 -109) was combined with immunoabsorption by different monoclonal antibodies directed against pancreatic phospholipase A 2 . Pancreatic phospholipase A 2 was purified from human duodenal juice. Monoclonal antibodies were prepared by fusion of spleen cells from immunized mice with P3X63-Ag8-653 myeloma cells. Samples with phospholipase A 2 activity were incubated in monoclonal antibody-coated microtitre plates. Phospholipase A 2 activities were determined in the monoclonal antibody-treated samples as well as in control samples. The method allows the determination of the fraction of human phospholipase A 2 isoenzymes in various biological materials. For pancreatic phospholipase A 2 the specific binding capacity was about 60 -80%, the unspecific binding was 5 -30%. Practically no crossreactivity was seen with partially purified serum phospholipase A 2 , with recombinant platelet phospholipase A 2 , or with the sera of patients with non-pancreatic diseases. In conclusion, the present study confirmed the presence of pancreatic phospholipase A 2 in human duodenal juice and in the ascites of necrotizing pancreatitis. However, pancreatic isoenzyme was absent in non-pancreatic inflammatory diseases. Therefore, elevated phospholipase activities in non-pancreatic inflammatory diseases cannot be attributed to the pancreas.
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