Abstract
Euglobulin from bovine plasma or outdated human blood plasma was freed of interfering impurities and applied to the anode side of the paper curtain of a Beckman Spinco CP electrophoresis apparatus in a cold room. Background buffer was at pH 3.5. The first and second leading fractions (cathode side) were combined and they contained plasminogen with approximately 10 times the specific esterolytic and caseinolytic activities of the original euglobulin. Cohn Fraction III can be substituted for human euglobulin. Additional purification can be obtained by phosphate precipitation of the curtain products. The specific esterolytic and caseinolytic activities of purified bovine and human plasminogen preparations, as well as their starch gel electrophoresis patterns, are reported and discussed.
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