Morrison D C, Cochrane C G
J Exp Med. 1974 Sep 1;140(3):797-811. doi: 10.1084/jem.140.3.797.
Purified precursor Hageman factor has been demonstrated to bind to soluble bacterial lipopolysaccharide (LPS, endotoxin) isolated from Escherichia coli 0111:B4, and this complex has been shown to have the capacity to convert prekallikrein to its active form. In addition, LPS-activated Hageman factor substantially reduces clotting times in XII-deficient plasma. The capacity to activate Hageman factor has been demonstrated to reside in the lipid A region of the LPS molecule. Activation of Hageman factor by LPS contrasts with fluid-phase activation (e.g., by kallikrein or trypsin) in that no cleavage to lower molecular weight fragments occurs. High concentrations of LPS inhibit the activity of Hageman factor, probably by a direct LPS-Hageman factor interaction.
纯化的前激肽释放酶原已被证明能与从大肠杆菌0111:B4中分离出的可溶性细菌脂多糖（LPS，内毒素）结合，并且这种复合物已被证明有能力将前激肽释放酶转化为其活性形式。此外，LPS激活的前激肽释放酶原能显著缩短缺乏因子XII的血浆的凝血时间。已证明激活前激肽释放酶原的能力存在于LPS分子的脂质A区域。LPS对前激肽释放酶原的激活与液相激活（如由激肽释放酶或胰蛋白酶激活）不同，因为不会发生切割成低分子量片段的情况。高浓度的LPS可能通过LPS与前激肽释放酶原的直接相互作用来抑制前激肽释放酶原的活性。
