Inactivation of the elastase inhibitory activity of alpha 1 antitrypsin in fresh samples of synovial fluid from patients with rheumatoid arthritis.
The proteinase inhibitory ability of alpha 1 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 degrees C before analysis, which does not significantly alter the proportion of inactive alpha 1 antitrypsin. In rheumatoid synovial fluid the elastase inhibitory ability was disproportionately depressed relative to the immunochemically determined concentrations of alpha 1 antitrypsin.
Chidwick
K
K
Inflammation Group, London Hospital Medical College, UK.
Winyard
P G
PG
Zhang
Z
Z
Farrell
A J
AJ
Blake
D R
DR
D001172:Arthritis, Rheumatoid / Q000201:enzymology*; D004791:Enzyme Inhibitors / Q000378:metabolism*; D006801:Humans; D010003:Osteoarthritis / Q000201:enzymology; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors*; D013582:Synovial Fluid / Q000201:enzymology*; D000515:alpha 1-Antitrypsin / Q000032:analysis / Q000378:metabolism*
D004791:Enzyme Inhibitors; D000515:alpha 1-Antitrypsin; D010196:Pancreatic Elastase