Ogloblina O G, Ruanet V V, Kazakova O V, Paskhina T S
Biokhimiia. 1981 Apr;46(4):667-73.
The inhibitory effect of thermo- and acid-resistant inhibitor of trypsin, chymotrypsin and leukocyte proteinases (TASPI) from rabbit serum on the kininogenase activity of cathepsins D from different organs and tissues (human spleen and liver, chicken liver, spleen leukemic infiltrate from patients with myeloid leukemia) was revealed. The progressive mechanism of TASPI and cathepsins D complexation dependent on time and temperature was revealed. The rate constant of inhibition (ki) of chicken liver cathepsin D by TASPI at 37 degrees was 4,25.10(3)M-1 min-1. It was shown that the kininogenase activity of chicken liver cathepsin D was slightly inhibited by the basic pancreatic trypsin and kallikrein inhibitor from bovine organs (Kunitz type) and by soya bean trypsin inhibitor. The role of TASPI as regulator of cathepsins D activity under pathological conditions accompanied by lysosomal disintegration is discussed.
已发现兔血清中对胰蛋白酶、糜蛋白酶和白细胞蛋白酶具有耐热和耐酸性的抑制剂（TASPI）对来自不同器官和组织（人脾脏和肝脏、鸡肝脏、髓性白血病患者脾脏白血病浸润组织）的组织蛋白酶D的激肽原酶活性具有抑制作用。揭示了TASPI与组织蛋白酶D络合的时间和温度依赖性渐进机制。在37℃时，TASPI对鸡肝脏组织蛋白酶D的抑制速率常数（ki）为4.25×10³M⁻¹min⁻¹。结果表明，来自牛器官的碱性胰腺胰蛋白酶和激肽释放酶抑制剂（Kunitz型）以及大豆胰蛋白酶抑制剂对鸡肝脏组织蛋白酶D的激肽原酶活性有轻微抑制作用。讨论了TASPI在伴有溶酶体解体的病理条件下作为组织蛋白酶D活性调节剂的作用。
