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. 1991 Dec;50(12):915–916. doi: 10.1136/ard.50.12.915

Inactivation of the elastase inhibitory activity of alpha 1 antitrypsin in fresh samples of synovial fluid from patients with rheumatoid arthritis.

K Chidwick 1, P G Winyard 1, Z Zhang 1, A J Farrell 1, D R Blake 1
PMCID: PMC1004581  PMID: 1768159

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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