Enzymatic Activity in Human Synovial Fluid from Rheumatoid and Non-Rheumatoid Patients.

Abstract

SummaryEnzyme assays have been done on sonicated cells after separation from synovial fluid (I), supernatant synovial fluid (II), and sonicated whole synovial fluid including cells (III). 2 lysosomal enzymes (acid phosphatase and lysozyme), 2 glycolytic enzymes (lactic dehydrogenase and pyruvate kinase), and adenylate kinase levels were measured in each of the 3 samples from each synovial fluid. Rheumatoid and non-rheumatoid fluids were studied.Results suggested that lysozyme derived at least in part from connective tissue. Lysozyme released from suspended cells by sonication was partially inhibited by supernatant synovial fluid (both rheumatoid and non-rheumatoid), as was commercial egg-white lysozyme added to synovial fluid. Lactic dehydrogenase was inhibited somewhat by rheumatoid synovial fluid and by 2 gouty synovial fluids studied. Commercial lactic dehydrogenase added to rheumatoid and non-rheumatoid synovial fluid was partially inhibited by the rheumatoid and not by the non-rheumatoid fluid.