Abstract
SummaryCrude bovine plasminogen was activated to plasmin by trypsin, by chloroform treatment which allowed an autocatalytic type activation, or by chloroform treatment followed by rapid activation with a low level of trypsin. Since the last method was an efficient one, other proteases were tried in the place of trypsin. Pancreatin and partially purified bovine plasmin also activated crude plasminogen but chymotrypsin, ficin and papain did not. Trypsin was the best activator of the series tested. Partially purified plasmins activated by trypsin, chloroform, or chloroform-trypsin were lyophilized and compared with one another. The plasmins prepared by trypsin activation appeared to be more potent
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Schedule a callMore From: Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.)
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