Abstract
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.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Arthritis, Rheumatoid / enzymology*
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Chromatography
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Electrophoresis, Polyacrylamide Gel
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Epitopes / immunology
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Humans
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Hydrogen-Ion Concentration
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Isoelectric Point
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Molecular Weight
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Pancreas / enzymology
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Phospholipases / isolation & purification*
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Phospholipases A / immunology
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Phospholipases A / isolation & purification*
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Phospholipases A2
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Radioimmunoassay
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Substrate Specificity
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Synovial Fluid / enzymology*
Substances
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Epitopes
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Phospholipases
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Phospholipases A
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Phospholipases A2