Chidwick K, Winyard P G, Zhang Z, Farrell A J, Blake D R
Inflammation Group, London Hospital Medical College, UK.
Ann Rheum Dis. 1991 Dec;50(12):915-6. doi: 10.1136/ard.50.12.915.
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.
在23份类风湿性关节炎滑液样本、8份骨关节炎滑液样本和9份正常对照血清样本中测定了α1抗胰蛋白酶的蛋白酶抑制能力。对于每个样本,以猪胰弹性蛋白酶作为靶蛋白酶进行了详细的动力学分析。分析前,样本在4℃下保存少于24小时,这不会显著改变无活性α1抗胰蛋白酶的比例。在类风湿性滑液中,相对于免疫化学测定的α1抗胰蛋白酶浓度,弹性蛋白酶抑制能力被不成比例地抑制。