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J. Biochem, 1976, Vol. 80, No. 2 341-349
© 1976 Japanese Biochemical Society

research-article

Studies on Phospholipase A in Trimeresurus flavoviridis Venom III. Purification and Some Properties of Phospholipase A Inhibitor in Habu Serum

Hiroshi KIHARA

Research Institute of Tropical Medicine, Faculty of Medicine, Kagoshima University Setouchi-cho, Oshima-gun. Kagoshima 894–15

Phospholipase A [EC 3.1.1.4 [EC] ] inhibitor was purified from Habu (Trimeresurus flavoviridis) serum by gel filtration on Sephadex G-200, chromatography on DE-23 cellulose and affinity chromatography on a Sepharose 4B-phospholipase A column. By these procedures, a 31-fold increase in specific activity was attained with a yield of 15%. The purified material was homogeneous as judged by cellulose acetate and polyacrylamide gel electrophoresis. It had an apparent molecular weight of 100,000 as measured by gel filtration on Sephadex G-200. The purified inhibitor was stable for 20 min at 80° and was unstable below pH 6. It migrated before albumin in cellulose acetate electrophoresis and did not form any precipitin line with the crude venom or with purified phospholipase A in immunodiffusin tests. An 8-fold excess of the purified inhibitor by weight was required to inhibit completely both the egg yolk clearing action and the hemolytic action of phospholipase A.


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