Exner T, Vaasjoki R
Haematology Department, Westmead Hospital, Australia.
Thromb Haemost. 1988 Feb 25;59(1):40-4.
The protein C activator (PCA) detectable in the venom of Agkistrodon Contortrix Contortrix (ACCV, Southern Copperhead) by specific immunochromometric assay and anticoagulant activity has been isolated and partially characterized. Chromatography of the crude venom on SP-Sephadex followed by Con A Sepharose and finally on hydroxylapatite was necessary to achieve an electrophoretically - pure product. The isolated PCA is a single chain glycoprotein with strong positive charge and an apparent molecular weight of 36,000. It had an immediate-inhibiting effect on the activated partial thromboplastin time (APTT) of normal plasma with no noticeable effect on the prothrombin time. Its prolonging effect on the APTT was dependent on protein C and it appeared to interfere with the contact mechanism rather than with factors V and VIII. It had enzymatic activity on some tripeptide chromogenic substrates sensitive to thrombin and kallikrein. When mixed with normal plasma it generated activity on substrates sensitive to activated protein C and should be useful for studies of protein C.
通过特异性免疫比浊法在南方铜头蝮蛇（Agkistrodon Contortrix Contortrix，ACCV）毒液中检测到的蛋白C激活剂（PCA）及其抗凝活性已被分离并进行了部分特性鉴定。为了获得电泳纯的产物，粗毒液需先在SP-葡聚糖凝胶上进行色谱分离，然后通过伴刀豆球蛋白A琼脂糖凝胶，最后在羟基磷灰石上进行分离。分离出的PCA是一种单链糖蛋白，带强正电荷，表观分子量为36,000。它对正常血浆的活化部分凝血活酶时间（APTT）有即刻抑制作用，而对凝血酶原时间无明显影响。其对APTT的延长作用依赖于蛋白C，并且似乎干扰接触机制而非因子V和VIII。它对一些对凝血酶和激肽释放酶敏感的三肽显色底物具有酶活性。当与正常血浆混合时，它能在对活化蛋白C敏感的底物上产生活性，应有助于蛋白C的研究。
