Kaplan A P, Goetzl E J, Austen K F
J Clin Invest. 1973 Oct;52(10):2591-5. doi: 10.1172/JCI107451.
The conversion of plasminogen proactivator to plasminogen activator by Hageman factor fragments results in the generation of chemotactic activity for human neutrophils. This chemotactic activity can be distinguished from that generated by Hageman factor activation of prekallikrein and is demonstrable in plasma that is genetically deficient in prekallikrein (Fletcher factor deficiency). Both the plasminogen-activating activity and chemotactic activity produced by the interaction of Hageman factor fragments and plasminogen proactivator to yield plasminogen activator were inhibited by diisopropyl fluorophosphate (DFP) indicating an essential role for the enzymatic site in both these activities. The finding that the plasminogen proactivator tolerated a dose of DFP, which completely inactivated the plasminogen activator, reveals that the active site is protected in the precursor protein.
哈格曼因子片段将纤溶酶原激活剂前体转化为纤溶酶原激活剂，从而产生对人中性粒细胞的趋化活性。这种趋化活性可与由哈格曼因子激活前激肽释放酶所产生的趋化活性相区分，并且在遗传性缺乏前激肽释放酶（弗莱彻因子缺乏症）的血浆中也可得到证实。哈格曼因子片段与纤溶酶原激活剂前体相互作用产生纤溶酶原激活剂时所产生的纤溶酶原激活活性和趋化活性均被二异丙基氟磷酸（DFP）抑制，这表明酶位点在这两种活性中均起重要作用。纤溶酶原激活剂前体能够耐受一定剂量的DFP，而该剂量可使纤溶酶原激活剂完全失活，这一发现表明活性位点在前体蛋白中受到保护。
