Comparison of textilinin-1 with aprotinin as serine protease inhibitors and as antifibrinolytic agents.

نویسندگان

  • Simone Flight
  • Lambro Johnson
  • Manuela Trabi
  • Patrick Gaffney
  • Martin Lavin
  • John de Jersey
  • Paul Masci
چکیده

Textilinin-1 (Q8008) was isolated from the venom of the Pseudonaja textilis and has a 47% sequence identity to the antihaemorrhagic therapeutic agent aprotinin. When equimolar concentrations of enzyme and aprotinin were pre-incubated, plasmin was inhibited 100%, plasma kallikrein 58%, and tissue kallikrein 99%. Under the same conditions, textilinin-1 inhibited plasmin 98%, plasma kallikrein 16% and tissue kallikrein 17%. Whole blood clot lysis was inhibited strongly by both aprotinin and textilinin-1, as shown by thrombelastography. At 2 microM inhibitor lysis initiated by t-PA was greater than 99% inhibited by aprotinin (LY60 = 0.4 +/- 0.1) whereas textilinin-1, inhibited lysis by 91% (LY60 = 8.9 +/- 0.7). The same trend was found with the lysis of euglobulin fractions. From these data textilinin-1 appears to be a more specific plasmin inhibitor than aprotinin but aprotinin inhibits clot lysis to a greater extent.

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عنوان ژورنال:
  • Pathophysiology of haemostasis and thrombosis

دوره 34 4-5  شماره 

صفحات  -

تاریخ انتشار 2005