Shvachko L P, Kibirev V K, Gaĭda A V, Monastyrskiĭ V A, Magerovskiĭ Iu V
Ukr Biokhim Zh (1978). 1988 Jan-Feb;60(1):3-7.
Thrombin purification is conducted by biospecific chromatography on gramicidin C-silochrome C 80. Preparations possessing the fibrinogen-coagulating activity of 2500-3200 NIH units per 1 mg of protein and containing 98% of active sites are obtained. Data obtained from electrophoresis in PAAG with the presence of DS-Na show the alpha-thrombin content to be 96%; the admixture of beta-thrombin possessing no coagulating activity does not exceed 4%. The kinetic constants are presented for thrombin hydrolysis of tosyl-L-arginine methyl ester (TAME), benzoyl-L-arginine ethyl ester (BAEE) and chromogenic substrate S-2238. The addition of isopropanol increases sharply the stability of thrombin when storing it in the aqueous-salt solutions.
凝血酶的纯化通过在短杆菌肽C - 硅铬酸C 80上进行生物特异性色谱法来进行。获得了每1毫克蛋白质具有2500 - 3200 NIH单位纤维蛋白原凝固活性且含有98%活性位点的制剂。在十二烷基硫酸钠存在下聚丙烯酰胺凝胶电泳获得的数据表明，α - 凝血酶含量为96%；不具有凝血活性的β - 凝血酶的混合物不超过4%。给出了凝血酶水解甲苯磺酰 - L - 精氨酸甲酯（TAME）、苯甲酰 - L - 精氨酸乙酯（BAEE）和发色底物S - 2238的动力学常数。当在盐水溶液中储存时，添加异丙醇会显著提高凝血酶的稳定性。
