Abstract
Phospholipase A 2 (PLA 2) activity has now been identified in rheumatoid synovial fluids. This PLA 2 is a calcium-requiring protein of MW 11,000 with a neutral pH optimum. Its ativity was inhibited by high concentrations of Mg 2+, and by the active site-directed histidine reagent p-bromophenacyl bromide. Ionic and non-ionic detergents, or the sulfhydryl reagent dithiothreitol caused loss of enzyme activity. Synovial fluid PLA 2 did not interact with sulphated mucopolysaccharides such as heparin or chondroitin sulphate. Release and sequestration of PLA 2 in the joint space may contribute to the characteristic rheumatoid inflammatory changes.
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