Purification of plasminogen
AssigneeArmour Pharmaceutical Company
InventorRobert M. Silverstein
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Abstract
The purification of plasminogen from human and non-human mammalian plasma or Cohn Fraction III by modified affinity chromotography using Sepharose-L-lysine with high ionic strength buffer solutions as in ion exchange chromatography is described. A plasminogen is produced in great yield having unexpectedly enhanced activity toward N.sup..alpha.-CBZ-L-lysine p-nitrophenyl ester, enhanced fibrinolytic activity and significantly less contamination by unknown colloidal substances.
Claims3
In the affinity chromatography method of isolating and purifying plasminogen from mammalian and human plasmas and Cohn III fractions comprising the steps of extracting the plasminogen, supplying the plasminogen-bearing extract to a L-lysine sepharose column, washing said column to elute impurities and then eluting the plasminogen, the improvement to the method comprising using a solution comprising about 0.5 molar sodium chloride in the step of washing the column.
Dependencies are inferred from the claim text.