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DOI: 10.1055/s-0037-1614954
Alboaggregins A and B. Structure and Interaction with Human Platelets
Publikationsverlauf
Received
16. Juni 1997
Accepted after revision
05. November 1997
Publikationsdatum:
07. Dezember 2017 (online)
![](https://www.thieme-connect.de/media/10.1055-s-00035024/199803/lookinside/thumbnails/10-1055-s-0037-1614954-1.jpg)
Summary
Viper venoms contain a variety of platelet binding proteins including those which bind to platelet GPIb/GPIX. Most of these proteins inhibit von Willebrand factor mediated platelet agglutination. Here we report the primary structures of unique members of this family, alboaggregins A and B, isolated from Trimeresurus albolabris, which have the ability to stimulate platelet agglutination and aggregation. Four chains of alboaggregin A and two chains of alboaggregin B share a high degree of homology and all cysteines in both alboaggregins are conserved. Both alboaggregins caused similar agglutination of fixed platelets. Alboaggregin A induced platelet aggregation and release reaction with EC50 = 10 and 30 nM, respectively, which is 20-fold lower than those for alboaggregin B. These observations suggest that the dimeric structure of alboaggregin B is sufficient to mediate its binding to GPIb and induce agglutination of platelets whereas aggregation and release reaction are significantly enhanced by tetrameric structure of alboaggregin A.
* Present address: M. A. Kowalska, Department of Hematology, Children’s Hospital of Philadelphia, Philadelphia, PA, USA
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