The effect of chemical anti-inhibitors on fibrinolytic enzymes and inhibitors

Clinica Chimica Acta; International Journal of Clinical Chemistry
J SidelmannJ Gram

Abstract

Fibrinolytic enzyme inhibitors hamper the determination of the specific fibrinolytic serine protease activity. Reportedly, chemical anti-inhibitors eliminate the influence of fibrinolytic inhibitors, but it remains unclear to what extent they change the specific activity of fibrinolytic serine proteases. We studied the influence of chemical anti-inhibitors (chloramine T, flufenamate, sodium lauryl sulfate, and methylamine) on fibrinolytic serine proteases and fibrinolytic enzyme inhibitors using the physiological substrate fibrin as plasmin substrate. Low concentrations of chloramine T (0.01 mmol/l) prevent the inhibition of plasminogen activators. Higher concentrations (1 mmol/l) reduce the inhibition of plasmin, but simultaneously quench the plasminogen activator activity. Flufenamate eliminates most fibrinolytic enzyme inhibitors, but increases the activity of plasmin (apparent recovery 140%) and plasminogen activators (apparent recovery > 200%). Sodium lauryl sulfate eliminates the major fibrinolytic enzyme inhibitors, but increases the activity of plasmin (apparent recovery > 200%) and plasminogen activator, urokinase type (apparent recovery 130%). Methylamine affects only plasmin inhibition. We conclude that chemical anti...Continue Reading

References

Dec 1, 1976·The Biochemical Journal·S Müllertz, I Clemmensen
Oct 7, 1975·Biochemistry·Y ShechterA Patchornik
Jun 1, 1985·Thrombosis Research·M H Chevallet-PrandiniM Suscillon
Jan 1, 1983·Annals of the New York Academy of Sciences·J B HowardE Eccleston

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