Abstract
Summary
Plasmin hydrolysis of casein was inhibited by DFP with the formation of DIP-plasmin. DIP-plasmin was able to react with SK to form a bovine plasminogen activator complex which was equal in activity to the complex formed between similar amounts of non-DFP-treated plasmin and SK. Plasmin-SK once formed, however, was subsequently inhibited by DFP. Since DIP-plasmin retains bovine plasminogen activator potential, it would appear that a DFP-inhibitable site other than that in plasmin is responsible for this activator potential.
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