Abstract
The properties of the one-chain and two-chain forms of the porcine tissue plasminogen activator have been compared with respect to their amidolytic activities against a low molecular weight synthetic substrate, and their inhibition by diisopropylphosphofluoridate, α 2-antiplasmin and C1-esterase inhibitor. The two-chain form is the more efficient catalyst, and is more rapidly inhibited by diisopropylphosphofluoridate and α 2-antiplasmin. Physiological implications are discussed.
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