Abstract
Purification of plasmin inhibitors of human plasma by ion-exchange chromatography on DEAE-Sephadex and by electrophoresis on starch-gel is described. The purified material was found to be an α1-globulin, heat and acid labile and containing 8% carbohydrates. A mol. wt. of 55 000 was calculated from a sedimentation constant of 3.3 and a diffusion constant of 5.2. The purified inhibitor exhibited both "slow" and "immediate" antiplasmin activities.
| Original language | English |
|---|---|
| Pages (from-to) | 35-41 |
| Number of pages | 7 |
| Journal | BBA - General Subjects |
| Volume | 121 |
| Issue number | 1 |
| DOIs | |
| State | Published - May 26 1966 |
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