Exposure of neutmphik to a variety of stimuli fin-&ding conunavalin A plus cytochalasi~ E) activates a membnne-bound NADPHoxidase to catalyst the gnemtion of the superoside anion radical (O;-t Rbhrr*rti~&s: q-AT. a,-antitrypsinr TPCK. L-l-tosylamide 3phenylahyl chloromethyl ketone: SBTI. soybean tqpsin inhibitor: Con A. connnovalin A: Cyto E. cytochalasin E.
The proteinase inhibitory ability of a, antitrypsin was measured in 23 samples of rheumatoid arthritis synovial fluid, eight osteoarthritic synovial fluids and nine normal control serum samples. For each sample a detailed kinetic analysis was performed with porcine pancreatic elastase as the target proteinase. Samples were stored for less than 24 hours at 4°C before analysis, which does not significantly alter the proportion of inactive a, antitrypsin. In rheumatoid synovial fluid the elastase inhibitory ability was disproportionately depressed relative to the immunochemically determined concentrations of a, antitrypsin.
Results and discussionNormal serum contained 3-74 (1-50) (mean (SD)) mg/ml a, antitrypsin. As expected, the 915 on 30 April 2019 by guest. Protected by copyright.
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