Teppo A M, Maury C P, Wegelius O
Scand J Immunol. 1982 Oct;16(4):309-14. doi: 10.1111/j.1365-3083.1982.tb00728.x.
Radial diffusion in agarose gel containing amyloid A (AA) fibrils was used to study the serum enzyme capable of degrading AA fibrils in vitro. This degradative activity was unaffected by soya bean trypsin inhibitor, tosyl-lysine chloromethyl ketone, and gold thiomalate but was inhibited by bovine pancreatic trypsin inhibitor, phenylmethylsulphonylfluoride, diisopropyl fluorophosphate, alpha 1-antitrypsin, and alpha 2-macroglobulin, indicating that the enzyme involved is a serine protease. Agarose gel electrophoresis showed the enzyme to be an acidic protein with the same electrophoretic mobility as albumin. The molecular weight, measured by gel filtration, was approximately 50,000. The optimum pH of this enzyme was 7.3, and it was fairly heat-resistant. The results suggest that the AA-fibril-degrading activity in human serum is due neither to elastase nor to cathepsin G. It has many characteristics in common with the enzymes unlike elastase that are involved in the complete degradation of serum AA protein.
利用淀粉样蛋白A（AA）纤维在琼脂糖凝胶中的径向扩散来研究能够在体外降解AA纤维的血清酶。这种降解活性不受大豆胰蛋白酶抑制剂、甲苯磺酰赖氨酸氯甲基酮和硫代苹果酸金的影响，但受到牛胰蛋白酶抑制剂、苯甲基磺酰氟、二异丙基氟磷酸、α1-抗胰蛋白酶和α2-巨球蛋白的抑制，表明所涉及的酶是一种丝氨酸蛋白酶。琼脂糖凝胶电泳显示该酶是一种酸性蛋白，其电泳迁移率与白蛋白相同。通过凝胶过滤测量，其分子量约为50,000。该酶的最适pH为7.3，且相当耐热。结果表明，人血清中的AA纤维降解活性既不是由弹性蛋白酶也不是由组织蛋白酶G引起的。它与参与血清AA蛋白完全降解的不同于弹性蛋白酶的酶有许多共同特征。
