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2000
Volume 14, Issue 5
  • ISSN: 0929-8665
  • E-ISSN: 1875-5305

Abstract

A novel disintegrin, stejnin, was purified from the Trimeresurus stejnegeri venom by gel filtration and reverse phase high performance liquid chromatography. The molecular weight of stejnin was determined to be 7428 Da by MALD-TOF MS analysis. The cDNA encoding the precursor of stejnin was cloned from the venom gland. From the deduced amino acid sequence, stejnin is composed of 71 amino acid residues contains the tripeptide sequence Arg-Gly-Asp (RGD), a well-known characteristic of the disintegrin family. Stejnin strongly inhibited ADP- and ristomycin-induced human platelet aggregation with IC50 of 45 and 50 nM, respectively. Stejnin also possessed potent inhibited cell proliferation of ECV304 cells.

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/content/journals/ppl/10.2174/092986607780782740
2007-05-01
2025-05-23
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/content/journals/ppl/10.2174/092986607780782740
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  • Article Type:
    Research Article
Keyword(s): disintegrin; ecv cells; platelet aggregation; snake venom
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