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Thrombolytic potency of acid‐stabilized plasmin: superiority over tissue‐type plasminogen activator in an in vitro model of catheter‐assisted thrombolysis
Author(s) -
Novokhatny V.,
Taylor K.,
Zimmerman T. P.
Publication year - 2003
Publication title -
journal of thrombosis and haemostasis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.947
H-Index - 178
eISSN - 1538-7836
pISSN - 1538-7933
DOI - 10.1046/j.1538-7836.2003.00128.x
Subject(s) - plasmin , thrombolysis , potency , in vitro , plasminogen activator , tissue plasminogen activator , medicine , chemistry , pharmacology , activator (genetics) , biochemistry , receptor , enzyme , myocardial infarction
Summary. Plasmin, the direct fibrinolytic enzyme, was compared with tissue plasminogen activator (t‐PA) in an in vitro thrombolysis model. Plasmin has been prepared in a highly pure form from human plasma and has been stabilized against auto‐degradation by low‐pH formulation. This acidified formulation of plasmin has been designed to have a low buffering capacity so that it can be directly infused into clots in a stable and latently active form. This low‐pH formulation has been shown to be equivalent to a neutral‐pH formulation of plasmin in its extent of clot lysis. An in vitro model of catheter‐assisted thrombolysis has been devised in which large (12 × 0.6 cm), retracted clots are treated with an intrathrombus thrombolytic agent via a multi‐sideport catheter. Plasmin dissolves these plasminogen‐deficient clots in a dose‐dependent manner and is clearly superior to t‐PA. In this model system, t‐PA exhibits efficacy only when retracted clots are replenished with plasminogen.