Pusey M L, Mende T J
Thromb Res. 1985 Aug 1;39(3):355-68. doi: 10.1016/0049-3848(85)90231-2.
A fraction of human amniotic fluid possessing procoagulant activity was purified 35-70 fold by gel filtration on Sepharose 4B. The activity eluted in the void volume indicating a particle size in excess of 5 X 10(6) daltons. The amniotic fluid factor (AFF) activity is stabilized on storage in the presence of Ca++ ions which could not be replaced by Mg++. Addition of phospholipids resulted in accelerated loss of activity. Steps taken to remove factor VII did not affect the activity, but factor X and V are required.
通过在琼脂糖4B上进行凝胶过滤，将具有促凝活性的一部分人羊水纯化了35至70倍。活性在空体积中洗脱，表明颗粒大小超过5×10⁶道尔顿。羊水因子（AFF）活性在有Ca²⁺离子存在的情况下储存时稳定，Mg²⁺不能替代Ca²⁺。添加磷脂会导致活性加速丧失。去除因子VII的步骤不影响活性，但需要因子X和V。
