1989 Volume 105 Issue 3 Pages 395-399
Extracellular phospholipase A2 was purified about 1.7×105 fold to near homogeneity from human synovial fluid of rheumatoid arthritis by sequential use of column chromatogra-phies on heparin-Sepharose, butyl-Toyopearl, and reversed-phase HPLC. The final prepa-ration showed a single band on SDS-polyacrylamide gel electrophoresis, and its molecular mass was estimated to be approximately 13, 700 daltons. The purified enzyme had a pH optimum of 9.0 and required Ca2+ for maximum activity. It hydrolyzed phosphatidyl-ethanolamine more effectively than phosphatidylserine and phosphatidylcholine. These properties were similar to those of an extracellular phospholipase A2 detected in the peritoneal cavity of caseinate-treated rats.
