Purification of a soluble phospholipase A2 from synovial fluid in rheumatoid arthritis.
A soluble phospholipase A2 (PLA2) was purified 4,500-fold from human rheumatoid synovial fluid. Preparative sodium dodecyl sulfate polyacrylamide gel electrophoresis yielded two bands of PLA2 activity of molecular weights 15,000 and 17,000 and pl 4.2-5.0. Purified PLA2 had absolute 2-acyl specificity, and hydrolyzed phosphatidylcholine with optimal activity at pH 7.5-8.0 and phosphatidylethanolamine with optimal activity at pH 7.0. Human synovial fluid PLA2 did not cross-react with anti-human pancreatic PLA2, as tested by radioimmunoassay.
D001172:Arthritis, Rheumatoid / Q000201:enzymology*; D002845:Chromatography; D004591:Electrophoresis, Polyacrylamide Gel; D000939:Epitopes / Q000276:immunology; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D008970:Molecular Weight; D010179:Pancreas / Q000201:enzymology; D010740:Phospholipases / Q000302:isolation & purification*; D010741:Phospholipases A / Q000276:immunology / Q000302:isolation & purification*; D054467:Phospholipases A2; D011863:Radioimmunoassay; D013379:Substrate Specificity; D013582:Synovial Fluid / Q000201:enzymology*
D000939:Epitopes; D010740:Phospholipases; D010741:Phospholipases A; D054467:Phospholipases A2