Deutsch D G, Mertz E T
Science. 1970 Dec 4;170(3962):1095-6. doi: 10.1126/science.170.3962.1095.
Plasminogen was prepared from human plasma by affinity chromatography on L-lysine-substituted Sepharose. Thirty milligrams of plasminogen, with a specific activity of 100 caseinolytic units (Committee on Thrombolytic Agents) per milligram of nitrogen, were obtained from 340 milliliters of plasma. This corresponds to over 200-fold purification from plasma. Disc-gel electrophoresis at pH 8.3 indicated seven distinct bands, all of which contained activity.
通过在L-赖氨酸取代的琼脂糖凝胶上进行亲和层析从人血浆中制备纤溶酶原。从340毫升血浆中获得了30毫克纤溶酶原，其比活性为每毫克氮100酪蛋白溶解单位（溶栓剂委员会）。这相当于从血浆中纯化了200多倍。在pH 8.3条件下进行的圆盘凝胶电泳显示有七条不同的条带，所有条带均具有活性。
