3d65

Structural highlights

Function

[IVBI1_PSETT] Strongly inhibits plasmin and trypsin. Has little effect on plasma and tissue kallikrein. Has no effect on tissue plasminogen inhibitor (t-PA), urokinase, activated protein C (APC) and elastase. Strongly inhibits whole blood clot lysis.^{[1] [2] [3] [4]}

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

• Trypsin

References

1. ↑ Filippovich I, Sorokina N, Masci PP, de Jersey J, Whitaker AN, Winzor DJ, Gaffney PJ, Lavin MF. A family of textilinin genes, two of which encode proteins with antihaemorrhagic properties. Br J Haematol. 2002 Nov;119(2):376-84. PMID:12406072
2. ↑ Masci PP, Whitaker AN, Sparrow LG, de Jersey J, Winzor DJ, Watters DJ, Lavin MF, Gaffney PJ. Textilinins from Pseudonaja textilis textilis. Characterization of two plasmin inhibitors that reduce bleeding in an animal model. Blood Coagul Fibrinolysis. 2000 Jun;11(4):385-93. PMID:10847427
3. ↑ Flight S, Johnson L, Trabi M, Gaffney P, Lavin M, de Jersey J, Masci P. Comparison of textilinin-1 with aprotinin as serine protease inhibitors and as antifibrinolytic agents. Pathophysiol Haemost Thromb. 2005;34(4-5):188-93. PMID:16707925 doi:http://dx.doi.org/10.1159/000092421
4. ↑ Flight SM, Johnson LA, Du QS, Warner RL, Trabi M, Gaffney PJ, Lavin MF, de Jersey J, Masci PP. Textilinin-1, an alternative anti-bleeding agent to aprotinin: Importance of plasmin inhibition in controlling blood loss. Br J Haematol. 2009 Apr;145(2):207-11. doi: 10.1111/j.1365-2141.2009.07605.x., Epub 2009 Feb 22. PMID:19236611 doi:http://dx.doi.org/10.1111/j.1365-2141.2009.07605.x