Preparation, Characterization, and Activation of a Highly Purified Factor XI: Evidence that a Hitherto Unrecognized Plasma Activity Participates in the Interaction of Factors XI and XII
Preparation, Characterization, and Activation of a Highly Purified Factor XI: Evidence that a Hitherto Unrecognized Plasma Activity Participates in the Interaction of Factors XI and XII
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高纯度因子 XI 的制备、表征和激活：迄今为止尚未识别的血浆活性参与因子 XI 和 XII 相互作用的证据
DOI：
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发表时间：
1974
影响因子：
6.5
通讯作者：
P. Lee
中科院分区：
文献类型：
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作者：
S. Schiffman;P. Lee
总结。用五步纯化方案从正常血浆中制备了高纯度的天然因子XI。纯化的因子XI基本上不含因子II、V、VII、VIII、IX、X、XII和Fletcher因子。未检测到纤溶酶原-纤溶酶。纯化的凝血因子XI腐烂迅速，但可以用人血清白蛋白稳定。在淀粉块电泳法上，XI因子在β和γ球蛋白之间迁移。经凝胶过滤，其表观分子量为210 000。纯化的凝血因子XI被弱胰酶激活。没有可检测到的BAEe酯酶活性伴随着这种激活。吸附在高岭土上的凝血因子XII和溶液中活化的凝血因子XII都不能激活纯化的凝血因子XI，两种试剂都能激活稀缺凝血因子XII的血浆中的凝血因子XI。因此，血浆似乎提供了促进因子XI和XII相互作用的第三种活性。这个活度被证明不同于弗莱彻因子。
Summary. Highly purified native factor XI has been prepared from normal plasma using a five step purification scheme. Purified factor XI is essentially free of factors II, V, VII, VIII, IX, X, XII, and Fletcher factor. No plasminogen‐plasmin could be detected. Purified factor XI decays rapidly but can be stabilized with human serum albumin. Factor XI migrates between the β and γ globulins on starch block electrophoresis. It has an apparent molecular weight on gel filtration of 210 000. Purified factor XI is activated by weak trypsin. No detectable BAEe esterase activity accompanies this activation. Neither factor XII adsorbed to kaolin nor activated factor XII in solution could activate purified factor XI; both reagents activate factor XI in dilute factor XII deficient plasma. Hence, plasma appears to supply a third activity which facilitates the interaction of factors XI and XII. This activity is shown to be distinct from Fletcher factor.