Plasminogen: purification from human plasma by affinity chromatography
DG Deutsch, ET Mertz - Science, 1970 - science.org
DG Deutsch, ET Mertz
Science, 1970•science.orgPlasminogen 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 p H 8.3 indicated seven distinct bands, all of which
contained activity.
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 p H 8.3 indicated seven distinct bands, all of which
contained activity.
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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