Baveux P, Bienvenu P, Beaudry Y, Frappa J, Fontanges R
C R Seances Soc Biol Fil. 1981;175(3):308-15.
Urokinase was obtained from cultured cells of human fetal kidneys. Ultrafiltration on an Amicon cell and purification by gel filtration chromatography (Ultrogel ACA54) yielded two molecules capable of activating plasminogen into plasmin. Their molecular weights were respectively 47,500 and 31,500 daltons. The first one showed more active than the latter. In this experiment, only small amounts of Urokinase were harvested. The yield could be enhanced using activators (pronase, glycine) or adapting fetal cells to large scale cultures.
尿激酶是从人胎肾培养细胞中获得的。通过在Amicon超滤器上进行超滤并经凝胶过滤色谱法(Ultrogel ACA54)纯化,得到了两种能够将纤溶酶原激活为纤溶酶的分子。它们的分子量分别为47,500和31,500道尔顿。第一种比第二种表现出更高的活性。在本实验中,仅收获了少量的尿激酶。使用激活剂(链霉蛋白酶、甘氨酸)或使胎儿细胞适应大规模培养可提高产量。