Drummond R K, Peppas N A
School of Chemical Engineering, Purdue University, West Lafayette, IN 47907.
Biomaterials. 1991 May;12(4):356-60. doi: 10.1016/0142-9612(91)90002-r.
Streptokinase was immobilized on poly(methacrylic acid-g-ethylene oxide) surfaces by means of a modified coupling reagent method. The surfaces were activated with a carbodiimide to form an O-acyl isourea derivative, which, upon addition of the enzyme, condensed to form the corresponding amide. The quantity of enzyme immobilized on the surface increased as the reaction time with carbodiimide and streptokinase increased. The fibrinolytic activity of the immobilized enzyme systems was measured by a clot lysis assay. The dynamics of fibrin clot lysis was investigated for a period of up to 500 min. The lysis reaction mechanism was found to approximate a first-order fibrin degradation. In addition, the kinetic rate constant was found to increase with increasing immobilized enzyme content.
通过改进的偶联试剂法将链激酶固定在聚（甲基丙烯酸 - g - 环氧乙烷）表面。先用碳二亚胺活化表面以形成O - 酰基异脲衍生物，加入酶后，该衍生物缩合形成相应的酰胺。随着与碳二亚胺和链激酶反应时间的增加，固定在表面的酶量增加。通过凝块溶解试验测定固定化酶系统的纤溶活性。研究了长达500分钟的纤维蛋白凝块溶解动力学。发现溶解反应机制近似于一级纤维蛋白降解。此外，发现动力学速率常数随着固定化酶含量的增加而增加。
