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A 28 kDa-protein with disintegrin-like structure (jararhagin-C) purified from Bothrops jararaca venom inhibits collagen- and ADP-induced platelet aggregation.
Department of Pharmaceutics, Gifu Pharmaceutical University, Japan.
A 28 kDa-protein with inhibitory activity on collagen- and ADP-induced platelet aggregation was purified from the venom of the snake Bothrops jararaca. Its complete amino acid sequence corresponded to the carboxyl-terminal region consisting of disintegrin-like and cysteine-rich domains of jararhagin, a high molecular weight hemorrhagic metalloprotease. Sequence homology of the protein to other disintegrins and disintegrin-like proteins from various snake venoms is also presented.
PMID: 8198592 [PubMed - indexed for MEDLINE]
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Cited by 5 PubMed Central articles
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A prothrombin activator from Bothrops erythromelas (jararaca-da-seca) snake venom: characterization and molecular cloning.
Silva MB, Schattner M, Ramos CR, Junqueira-de-Azevedo IL, Guarnieri MC, Lazzari MA, Sampaio CA, Pozner RG, Ventura JS, Ho PL, et al.
Biochem J. 2003 Jan 1; 369(Pt 1):129-39.
[Biochem J. 2003]
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Purification, molecular cloning and mechanism of action of graminelysin I, a snake-venom-derived metalloproteinase that induces apoptosis of human endothelial cells.
Wu WB, Chang SC, Liau MY, Huang TF.
Biochem J. 2001 Aug 1; 357(Pt 3):719-28.
[Biochem J. 2001]
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Antibody from mice immunized with DNA encoding the carboxyl-disintegrin and cysteine-rich domain (JD9) of the haemorrhagic metalloprotease, Jararhagin, inhibits the main lethal component of viper venom.
Harrison RA, Moura-Da-Silva AM, Laing GD, Wu Y, Richards A, Broadhead A, Bianco AE, Theakston RD.
Clin Exp Immunol. 2000 Aug; 121(2):358-63.
[Clin Exp Immunol. 2000]
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