Billingsley G D, Cox D W
Hum Genet. 1982;61(2):118-22. doi: 10.1007/BF00274200.
The specific activity of thirteen genetic variants of the protease inhibitor alpha 1-antitrypsin (alpha 1AT) has been determined. Elastase inhibitor activity was assayed protein substrates (elastin and gelatin) and the synthetic substrate N-tert-butoxy-carbonyl-L-alanine p-nitrophenyl ester. The synthetic substrate alpha-N-benzoyl-DL-arginine p-nitroanilide HCl was used to assay trypsin inhibitor activity. The specific activity of alpha 1AT was expressed as serum inhibition/immunological concentration of alpha 1AT. Sera of PI type FM had reduced specific activity with elastase, but not with trypsin. With the possible exception of MP, no other variants showed significant differences in specific activity when compared with normal PI type M.
已测定了蛋白酶抑制剂α1 - 抗胰蛋白酶（α1AT）的13种基因变体的比活性。用蛋白质底物（弹性蛋白和明胶）以及合成底物N - 叔丁氧羰基 - L - 丙氨酸对硝基苯酯测定弹性蛋白酶抑制活性。用合成底物α - N - 苯甲酰 - DL - 精氨酸对硝基苯胺盐酸盐测定胰蛋白酶抑制活性。α1AT的比活性以α1AT的血清抑制/免疫浓度表示。PI型FM血清对弹性蛋白酶的比活性降低，但对胰蛋白酶的比活性未降低。与正常PI型M相比，除了可能的MP型外，没有其他变体的比活性显示出显著差异。
