PLASMINOGEN - PURIFICATION FROM HUMAN PLASMA BY AFFINITY CHROMATOGRAPHY
PLASMINOGEN - PURIFICATION FROM HUMAN PLASMA BY AFFINITY CHROMATOGRAPHY
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DOI：
10.1126/science.170.3962.1095
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发表时间：
1970-01-01
期刊：
影响因子：
56.9
通讯作者：
MERTZ, ET
中科院分区：
文献类型：
--
作者：
DEUTSCH, DG;MERTZ, ET
通过L-赖氨酸取代的琼脂糖凝胶亲和层析从人血浆中制备纤溶酶原。从340毫升血浆中获得30毫克纤溶酶原，其比活性为每毫克氮100个酪蛋白溶解单位（血栓溶解剂委员会）。这相当于从血浆中纯化超过200倍。pH 8.3的圆盘凝胶电泳显示七条不同的条带，所有条带均含有活性。
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 atpH 8.3 indicated seven distinct bands, all of which contained activity.