Baskova I P, Tiero A, Krizhevskaia Iu V, Iarovaia G A, Mirkamalova E G
Biull Eksp Biol Med. 1983 Aug;96(8):13-6.
A study was made of the interaction between prothrombin and enzymes: blood plasma kallikrein and factors alpha-XIIa and beta-XIIa immobilized on enzacryl-AH. Kallikrein-induced prothrombin proteolysis was accompanied by a decrease in prothrombin activity, appearance of BAME-esterase and poor clotting activity. As a result of fractionation of products on the column with DEAE-Sephadex A-50, some fractions that have thrombin amidase activity (splitting of the substrate S-2238) and high antithrombin activity were obtained. Antithrombin activity manifested in the inhibition of fibrinmonomer aggregation during fibrin formation. During incubation with prothrombin, factors alpha-XIIa and beta-XIIa also stimulated the appearance of BAME-esterase activity. None of the immobilized enzymes activated factor X.
血浆激肽释放酶以及固定在恩扎丙烯-AH上的α-XIIa和β-XIIa因子。激肽释放酶诱导的凝血酶原蛋白水解伴随着凝血酶原活性降低、BAME酯酶出现以及凝血活性不佳。在用DEAE-葡聚糖A-50柱对产物进行分级分离后，获得了一些具有凝血酶酰胺酶活性（底物S-2238裂解）和高抗凝血酶活性的级分。抗凝血酶活性表现为在纤维蛋白形成过程中抑制纤维蛋白单体聚集。在与凝血酶原孵育期间，α-XIIa和β-XIIa因子也刺激了BAME酯酶活性的出现。没有一种固定化酶激活因子X。
