Sakamoto W, Yoshikawa K, Yokoyama A, Kohri M
Biochim Biophys Acta. 1986 Dec 10;884(3):607-9. doi: 10.1016/0304-4165(86)90216-3.
Using highly purified T-kininogen and cathepsin E-like proteinase and 72 kDa proteinase in rat spleen, the release of T-kinin from T-kininogen was found to occur by consecutive cleavage by cathepsin E-like proteinase and 72 kDa proteinase. 72 kDa proteinase seems to be serine proteinase, because it was completely inhibited by diisopropyl fluorophosphate but not by pepstatin, leupeptin and bestatin.
使用高度纯化的T-激肽原、类组织蛋白酶E样蛋白酶和大鼠脾脏中的72 kDa蛋白酶，发现T-激肽从T-激肽原的释放是通过类组织蛋白酶E样蛋白酶和72 kDa蛋白酶的连续切割而发生的。72 kDa蛋白酶似乎是丝氨酸蛋白酶，因为它完全被氟磷酸二异丙酯抑制，而不被胃蛋白酶抑制剂、亮抑酶肽和抑氨肽酶抑制。
