Summary
When urea or ε-amino caproic acid were used as solublizing agents for plasminogen
in electrophoretic experiments, only one broad band of the proenzyme was obtained
on acetate cellulose, in starch block, and in acrylamide gel. In starch gel electrophoresis,
however, both forms of plasminogen – the native or euglobulin and Kline’s or Pseudoglobulin
plasminogen – separated into six bands. These migrated toward the cathode at room
temperature in borate or veronal buffer in the alkaline range and showed full activity
in fibrinagar-streptokinase plates.
