Purification and characterization of phospholipase A2 released from rat platelets.
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概要
- 論文の詳細を見る
It was found that phospholipase A2 and lysophospholipase, both of which were released from thrombin-stimulated rat platelets, had high affinity to insolubilized heparin. Phospholipase A2 released from rat platelets was purified by the sequential use of column chromatography on heparin-Sepharose and TSK gel G2000SW (highperformance liquid chromatography, HPLC). The enzyme was near homogeneous on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and HPLC, and its Mr was estimated to be 13, 500. The purified enzyme was labile and lost its activity within 1h when incubated at 37°C. Phospholipids or detergent in the solution protected the enzyme against inactivation. Phospholipase activity was inhibited by p-bromophenacylbromide, but not by diisopropylfluorophosphate or iodoacetamide. Lysophospholipase, which was also released from rat platelets, was separated from phospholipase A2 by chromatography on heparin-Sepharose.
- 社団法人 日本生化学会の論文
著者
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Hayakawa Makio
Department Of Biochemistry Faculty Of Pharmaceutical Sciences Setsunan University
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Inoue Keizo
Department Of Biochemistry And Molecular Biology Indiana University
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Nojima Shoshichi
Department Of Health Chemistry Faculty Of Pharmaceutical Sciences The University Of Tokyo
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HORIGOME Kazuhiko
Department of Health Chemistry, Faculty of Pharmaceutical Sciences, The University of Tokyo
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