抄録
Phospholipase A [EC 3.1.1.4] inhibitor was purified from Habu (Trimeresurus favoviridis) 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 cel-lulose 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.
