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利用ＣＤ谱对皖南尖吻蝮蛇蛇毒内抗凝血因子（ＡＣＦ）的二级结构，即α－螺旋、β－折叠和无规则卷曲进行了测定，利用ＣｈｅｎａｎｄＹａｎｇ的方法计算出了它们在ＡＣＦ分子内的百分比．溶液的ｐＨ值对ＡＣＦ的二级结构影响不大，但当ｐＨ位于５和６时，二级结构稍稍出现了异常．这可能是由于氢离子电离引起的电荷变化带来的效应．ＡＣＦ的脱钙破坏了分子内的配位结构，而使α－螺旋的百分比大大降低．尽管三价镧系离子能取代ＡＣＦ中的钙离子，但是没有给ＡＣＦ的二级结构带来较大的影响．
The secondary structure of anticoagulant factor (ACF), namely, α-helix, β-sheet and random coil were detected by CD spectra and the ACF molecules were calculated by ChenandYang method Percentage within. The pH value of the solution had little effect on the secondary structure of the ACF, but the secondary structure was slightly abnormal at pH 5 and 6. This is probably due to the effect of charge changes due to hydrogen ionization. The decalcification of ACF destroys the intramolecular coordination structure and greatly reduces the percentage of α-helices. Although the trivalent lanthanide ions can replace the calcium ions in the ACF, they do not bring much influence on the secondary structure of ACF.