Comparison of textilinin-1 with aprotinin as serine protease inhibitors and as antifibrinolytic agents |
| |
Authors: | Flight Simone Johnson Lambro Trabi Manuela Gaffney Patrick Lavin Martin de Jersey John Masci Paul |
| |
Institution: | School of Medicine, University of Queensland, Princess Alexandra Hospital, Brisbane, Australia. |
| |
Abstract: | 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. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|