Abstract
Summary
Antiactivator activity of human serum, which inhibits activator-induced clot lysis, was separated from α1-antitrypsin by affinity chromatography on Sepharose coupled with IgG of antiserum to α1-antitrypsin. It was found that most of antiplasmin activity formerly found in the antiactivator fraction is actually due to α1-antitrypsin contaminating the fraction. Antiactivator itself has no or little antiplasmin activity. On the other hand, α1-antitrypsin possesses antiplasmin activity but has no antiactivator activity.
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