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  • Title: A new thrombin-like enzyme, flavoviridiobin from the venom of Trimeresurus flavoviridis (habu).
    Author: Tatematsu R, Komori Y, Nikai T.
    Journal: J Nat Toxins; 2000 Nov; 9(4):327-39. PubMed ID: 11126511.
    Abstract:
    Fibrinopeptide A and B releasing enzyme, flavoviridiobin, was isolated from the venom of Trimeresurus flavoviridis using Q-Sepharose, CM-Cellulose, and Sephadex G-75 column chromatographies. Homogeneity was established by the formation of a single band in polyacrylamide gel electrophoresis, isoelectric focusing, and Ouchterlony immunodiffusion. The enzyme has a molecular weight of 48,000, isoelectric point of 8.1, consists of 237 total amino acid residues, and demonstrates clotting activity. However, no tosyl-L-arginine methyl ester (TAME) hydrolytic and kinin-releasing activities were observed. This clotting enzyme was inhibited by p-amidinophenylmethanesulfonyl fluoride hydrochloride (p-APMSF), benzamidine, and beta-mercaptoethanol, suggesting that serine, acidic amino acids, and disulfide bonds are involved in the expression of the enzyme's clotting activity. This thrombin-like enzyme hydrolyzes B beta-chain of human fibrinogen at first, followed by hydrolysis A alpha-chain. The enzyme was stable over the pH range of 7-10 and was shown to be heat resistant.
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