Viana Carolina A, Oliveira Jefferson S, Freitas Cleverson D T, Alencar Nylane M N, Carvalho Cristina P S, Nishi Beatriz C, Ramos Márcio V
Department of Biochemistry and Molecular Biology, Federal University of Ceará, Fortaleza, CE, Brazil.
Blood Coagul Fibrinolysis. 2013 Jun;24(4):386-92. doi: 10.1097/MBC.0b013e32835d540b.
Latex proteins have drawn attention because they have shown several pharmacological activities. Herein, the fibrin(ogen)olytic activity of Cryptostegia grandiflora (CgLP) and Plumeria rubra (PrLP) latices were evaluated and characterized. Ion-exchange chromatography separated CgLP in proteolytic (CgLP PI) and nonproteolytic proteins (CgLP PII). CgLP and CgLP PI hydrolyzed azocasein in a dose-dependent manner, whereas CgLP PII and PrLP showed negligible activities. CgLP and CgLP PI accelerated plasmatic clot formation and digested all fibrinogen chains in a time/dose-dependent manner, though in a nonspecific way. CgLP and CgLP PI did not fully hydrolyze the subunits of the fibrin clot since fibrin α-chain showed resistance to proteolysis. No fibrinogenolytic activity was noticed after incubation of CgLP and CgLP PI with E-64. These results suggested that fibrinogenolytic and procoagulant activities of C. grandiflora were performed by cysteine proteases and confirm the activity of latex cysteine proteases as thrombin and plasmin-like proteins.
乳胶蛋白因其具有多种药理活性而备受关注。在此，对大花羊角拗（CgLP）和朱缨花（PrLP）乳胶的纤维蛋白（原）溶解活性进行了评估和表征。离子交换色谱法将CgLP分离为蛋白水解性蛋白（CgLP PI）和非蛋白水解性蛋白（CgLP PII）。CgLP和CgLP PI以剂量依赖性方式水解偶氮酪蛋白，而CgLP PII和PrLP的活性可忽略不计。CgLP和CgLP PI加速血浆凝块形成，并以时间/剂量依赖性方式消化所有纤维蛋白原链，尽管方式是非特异性的。CgLP和CgLP PI并未完全水解纤维蛋白凝块的亚基，因为纤维蛋白α链对蛋白水解具有抗性。将CgLP和CgLP PI与E-64孵育后未观察到纤维蛋白原溶解活性。这些结果表明，大花羊角拗的纤维蛋白原溶解活性和促凝血活性由半胱氨酸蛋白酶发挥作用，并证实乳胶半胱氨酸蛋白酶具有类似凝血酶和纤溶酶的活性。
