Mandle R J, Kaplan A P
Blood. 1979 Oct;54(4):850-62.
Human coagulation factor XI has been purified, and upon activation with Hageman factor fragments, was found to convert the fibrinolytic proenzyme plasminogen to plasmin. This proactivator activity was shown to be functionally and antigenically distinct from prekallikrein. When the gamma-globulin fractions of plasma deficient in Hageman factor, prekallikrein and factor XI were isolated, factor-XI-deficient plasma possessed two-thirds of the plasminogen proactivator activity of the Hageman-factor-deficient plasma, while prekallikrein deficient plasma had only one-third of the plasminogen proactivator activity. Thus, the Hageman-factor-dependent plasminogen proactivator previously reported to be present in the gamma-globulin fraction of normal human plasma is a function of prekallikrein and factor XI, while the activity observed in prekallikrein-deficient plasma is attributable to factor XI. When compared utilizing digestion of iodinated fibrin, prekallikrein and factor XIa had similar potency per active site; they were, however, far less active than urokinase.
人凝血因子XI已被纯化,在用Hageman因子片段激活后,发现它能将纤溶酶原激活为纤溶酶。这种前激活剂活性在功能和抗原性上与前激肽释放酶不同。当分离缺乏Hageman因子、前激肽释放酶和因子XI的血浆的γ球蛋白组分时,缺乏因子XI的血浆具有缺乏Hageman因子的血浆三分之二的纤溶酶原激活剂活性,而缺乏前激肽释放酶的血浆只有缺乏Hageman因子的血浆三分之一的纤溶酶原激活剂活性。因此,先前报道存在于正常人血浆γ球蛋白组分中的依赖Hageman因子的纤溶酶原激活剂是前激肽释放酶和因子XI的功能,而在缺乏前激肽释放酶的血浆中观察到的活性归因于因子XI。当利用碘化纤维蛋白的消化进行比较时,前激肽释放酶和因子XIa每个活性位点的效力相似;然而,它们的活性远低于尿激酶。