pH值和金属离子对尖吻蝮蛇抗凝血因子Ⅱ二级结构的影响  

The Effects of pH and Metal Ions on the Secondary Structure of Anticogulation Factor Ⅱ Studed by CD Spectroscopy

作　　者：陈结霞[1] 徐小龙[1] 刘祥虎[1] 刘清亮[1] 

机构地区：[1]中国科学技术大学化学系,合肥230026

出　　处：《无机化学学报》2006年第1期69-72,共4页Chinese Journal of Inorganic Chemistry

基　　金：国家自然科学基金资助项目(No.20571069;20171041)。

摘　　要：圆二色谱(CD谱)测量表明,尖吻蝮蛇抗凝血因子Ⅱ(ACFⅡ)与抗凝血因子Ⅰ(ACFⅠ)的二级结构十分相似,它们的主要骨架构象都为反平行β-折叠和α-螺旋结构。pH值对天然ACFⅡ的构象有一定的影响,pH值从3到10增大时,α-螺旋含量逐渐减少,反平行β-折叠含量逐渐增大。钙和其他二价金属离子对ACFⅡ的骨架结构没有明显影响。三价稀土离子使ACFⅡ的α-螺旋含量升高,同时降低其β-转角和β-折叠的含量。Anticoagulation factors holo-ACF Ⅱ and holo-ACF Ⅰ have similar secondary structures and their main backbone conformations are anti-parallel β-sheet and α-helix determined by CD spectra. The contents of antiparallel β-sheet and α-helix are 26.2%, 13.7% for holo-ACF Ⅱ, respectively. When pH value increases, the content of α-helix of ACF Ⅱ decreases, while the contents of anti-parallel β-sheet increases. No apparent effects of Ca^2＋, Sr^2＋, Mg^2＋ and transition metal ions （Zn^2＋, Mn^2＋ and Co^2＋） on conformations of the backbone of ACF Ⅱ are observed. The substitution of lanthanide ions for Ca^2＋ in ACF Ⅱ increases the content of α-helix, but decreases the content of β-sheet.

关 键 词：抗凝血因子Ⅱ 酸度(pH) 二级结构 圆二色谱 

分 类 号：O614.2[理学—无机化学] O614.33[理学—化学]