Title : A potent antiplatelet peptide, triflavin, from Trimeresurus flavoviridis snake venom.

Pub. Date : 1991 Jul 15

PMID : 1859363






5 Functional Relationships(s)
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1 Triflavin inhibited fibrinogen-induced aggregation of human elastase-treated platelets in a dose-dependent manner, indicating that it directly interferes with the binding of fibrinogen to its receptors on platelet membranes exposed by elastase treatment. triflavin fibrinogen beta chain Homo sapiens
2 Triflavin inhibited fibrinogen-induced aggregation of human elastase-treated platelets in a dose-dependent manner, indicating that it directly interferes with the binding of fibrinogen to its receptors on platelet membranes exposed by elastase treatment. triflavin fibrinogen beta chain Homo sapiens
3 Additionally, triflavin dose-dependently blocked 125I-labelled fibrinogen binding to ADP-activated platelets. triflavin fibrinogen beta chain Homo sapiens
4 In conclusion, triflavin inhibits platelet aggregation through the blockade of fibrinogen binding to fibrinogen receptors on platelet membranes. triflavin fibrinogen beta chain Homo sapiens
5 In conclusion, triflavin inhibits platelet aggregation through the blockade of fibrinogen binding to fibrinogen receptors on platelet membranes. triflavin fibrinogen beta chain Homo sapiens