TAGER M
J Exp Med. 1956 Nov 1;104(5):675-86. doi: 10.1084/jem.104.5.675.
The coagulase-reacting factor (CRF) of human plasma has been purified, concentrated, and largely freed of prothrombin activity by Seitz filtration, absorbtion on hyflo-amphogel columns, controlled phosphate buffer elution, and fractional ammonium sulfate precipitation. The purified CRF preparations localized between the beta and the gamma globulin position on paper electrophoresis, and the principal of two components observed on analytical ultracentrifugation gave sedimentation rates between 2.75 and 3.07. Highly purified prothrombin preparations of Seegers effectively react with staphylocoagulase to lead to the coagulation of plasma. The electrophoretic and ultracentrifugal properties of the human prothrombin preparations examined differ significantly from those of the purified CRF. Derivatives of prothrombin, involving a loss of prothrombin activity, such as thrombin and "autoprothrombin," do not correspondingly lose in CRF function. The hypothesis is proposed that CRF activity is resident in some component or components of the prothrombin molecule not involved in prothrombin function per se, and that therefore prothrombin and CRF activity may either parallel each other when the molecule is intact or diverge when the smaller units only are involved.
人血浆的凝固酶反应因子（CRF）已通过赛茨过滤、在海弗洛两性凝胶柱上吸附、控制磷酸盐缓冲液洗脱及分级硫酸铵沉淀进行了纯化、浓缩，并基本去除了凝血酶原活性。纯化后的CRF制剂在纸上电泳时位于β球蛋白和γ球蛋白之间，在分析超速离心中观察到的两种主要成分的沉降率在2.75至3.07之间。西格斯的高纯度凝血酶原制剂能有效地与葡萄球菌凝固酶反应，导致血浆凝固。所检测的人凝血酶原制剂的电泳和超速离心特性与纯化后的CRF有显著差异。凝血酶原的衍生物，如凝血酶和“自身凝血酶原”，虽然失去了凝血酶原活性，但CRF功能并没有相应丧失。有人提出这样的假说：CRF活性存在于凝血酶原分子中一些本身不参与凝血酶原功能的成分中，因此当分子完整时，凝血酶原和CRF活性可能相互平行，而当仅涉及较小单位时则可能出现差异。
