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Science 4 December 1970:
Vol. 170. no. 3962, pp. 1095 - 1096
DOI: 10.1126/science.170.3962.1095

Articles

Plasminogen: Purification from Human Plasma by Affinity Chromatography

Dale G. Deutsch 1 and Edwin T. Mertz 1

1 Department of Biochemistry, Purdue University, Lafayette, Indiana 47907

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.


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