Abstract:Comparative studies were made on eleven urokinase preparations commercially available. Analysis by both gel filtration and sodium dodecyl gel electrophoresis revealed the variety of molecular forms of the activator in the preparations showing molecular weight approximately 54,000 (A), 47,000 (B) and 34,000 (C). Starch gel electrophoresis at pH 8.8 indicated that (B) and (C) moved to anode whereas (A) and the active component of fresh urine slightly moved to the cathod. Proteolytic digestion of (A) produced the… Show more
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