Benavent A, Estellés A, Aznar J, Martinez-Sales V, Gilabert J, Fornas E
Thromb Haemost. 1984 Feb 28;51(1):67-70.
The functional activity and active site of plasmin in full-term newborns have been studied and compared to those in adults in order to investigate the nature of the abnormality found in newborn plasminogen described in a previous paper. The functional activity of newborn plasminogen measured on chromogenic substrate was approximately 18% that of adult plasminogen when streptokinase was used as an activator and 12% when urokinase was used. Proteolysis of newborn plasminogen by urokinase yielding a two-chain plasmin form occurred normally, but the incorporation of diisopropylphosphorofluoridate into the light chain of newborn plasmin was approximately 23% of that observed in the light chain of adult plasmin. These observations suggest that the abnormality of full-term newborn plasminogen is located in the active site of the molecule.
为了研究前文所述新生儿纤溶酶原异常的本质，对足月儿纤溶酶的功能活性和活性位点进行了研究，并与成人的进行了比较。当使用链激酶作为激活剂时，在发色底物上测得的新生儿纤溶酶原的功能活性约为成人纤溶酶原的18%；当使用尿激酶时，该活性约为成人纤溶酶原的12%。尿激酶对新生儿纤溶酶原进行蛋白水解生成双链纤溶酶形式的过程正常，但二异丙基氟磷酸酯掺入新生儿纤溶酶轻链的量约为成人纤溶酶轻链的23%。这些观察结果表明，足月儿纤溶酶原的异常位于分子的活性位点。
