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J. Biochem, 1983, Vol. 94, No. 1 137-147
© 1983 Japanese Biochemical Society

research-article

Purification and Characterization of Human Pancreatic Phospholipase A2 and Development of a Radioimmunoassay1

Junichi NISHIJIMA*, Mitsuhiro OKAMOTO**, Michio OGAWA*, Goro KOSAKI* and Toshio YAMANO**

*Second Department of Surgery, Osaka University Medical School Fukushima-ku, Osaka 553
**Department of Biochemistry, Osaka University Medical School Kita-ku, Osaka 530

Human pancreatic phospholipase A2, was purified to homogeneity from pancreatic juice and a reliable radioimmunoassay for the enzyme was developed. The molecular weight of the enzyme as estimated by sodium dodecyl sulfate polyacrylamide gel electrophoresis was 14,000. Phosphatidylcholine was hydrolyzed well in an alkaline pH range, and the optimum activity was obtained at pH 9. Calcium ion was indispensable for activity. The enzyme was stable to heat treatment at 60°C for 5 min.

The radioimmunoassay system was highly sensitive, reproducible and specific. The dilution curves for the sera of patients with acute pancreatitis were parallel to the standard curve. In healthy individuals, serum phospholipase A2, concentrations ranged from 2.0 to 7.9 ng/ml, the average being 5.1 ng/ml (S.D.: 1.7). In patients with acute pancreatitis, significant elevations of serum phospholipase A, contents were observed, and the highest value found was 4,000 ng/ml.

1This work was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan (No. 57213023).


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