Abstract

Abstract A method is described for removal of heparin from aqueous solutions. Poly(L-lysine) covalently linked to Sepharose 4B has a strong affinity for heparin. Passage of an aqueous heparin solution through a column of poly(L-lysine)-Sepharose 4B (PLLS) results in complete removal of heparin under appropriate experimental conditions. Heparin adsorbed to PLLS then can be eluted quantitatively from the column by addition of 0.1 N NaOH. No significant loss in anticoagulant properties is observed in heparin eluted from PLLS. PLLS can be used to remove heparin from plasma also. Following exposure to plasma containing heparin, PLLS can be washed with solutions of high ionic strength, low pH, or both to remove most nonspecifically adsorbed plasma proteins. Analysis by crossed immunoelectrophoresis of heparin eluted from PLLS showed that the anticoagulant recovered contained less than 1 μg of albumin/ml (0.001% of plasma albumin) but apparently was free of other plasma proteins. Washing of PLLS with solutions of high ionic strength and low pH probably resulted in the loss of certain blood coagulation factors (factors VIII and XII), while the concentration of factor X and antithrombin III did not change appreciably.

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