Shimizu A, Jimenez E C, Takagi J, Inada Y, Saito Y
Laboratory of Biological Chemistry, Tokyo Institute of Technology, Japan.
Toxicon. 1987;25(7):751-7. doi: 10.1016/0041-0101(87)90125-5.
Using gel permeation chromatography with high performance liquid chromatograph (HPLC), a highly purified preparation of a protease has been obtained from the venom of the southern copperhead snake (Agkistrodon contortrix contortrix). Both gel permeation chromatography with HPLC and sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed that it had an apparent Mr of 60,000-64,000. It consisted of a single polypeptide chain. The activity was inhibited by dithiothreitol. It neither induced platelet aggregation nor activated plasma factor XIII. It cleaved fibrinopeptide B at a rate much faster than fibrinopeptide A from fibrinogen. This specificity was steadily lowered when the incubation temperature was elevated from 0 degrees C to 45 degrees C. Fibrinopeptides were released only at neutral pH.
使用配备高效液相色谱仪（HPLC）的凝胶渗透色谱法，从南方铜头蝮蛇（Agkistrodon contortrix contortrix）的毒液中获得了一种高度纯化的蛋白酶制剂。HPLC凝胶渗透色谱法和十二烷基硫酸钠-聚丙烯酰胺凝胶电泳均显示其表观分子量为60,000 - 64,000。它由一条单一的多肽链组成。其活性受到二硫苏糖醇的抑制。它既不诱导血小板聚集，也不激活血浆因子XIII。它从纤维蛋白原中切割纤维蛋白肽B的速度比切割纤维蛋白肽A的速度快得多。当孵育温度从0℃升高到45℃时，这种特异性会稳步降低。纤维蛋白肽仅在中性pH值下释放。
