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• W2014128212 abstract "The development of thrombin inhibitors could provide invaluable progress for antithrombotic therapy. In this paper, we report the cloning, purification and biochemical characterization of dipetarudin, a chimeric thrombin inhibitor composed of the N-terminal head structure of dipetalogastin II, the strongest inhibitor from the assassin bug Dipetalogaster maximus, and the exosite 1 blocking segment of hirudin, connected through a five glycine linker. The cloning of dipetarudin was performed by a simple method which had not been used previously to clone chimeras. Biochemical characterization of dipetarudin revealed that it is a slow, tight-binding inhibitor with a molecular mass (M(r)=7560) and a thrombin inhibitory activity (K(i)=446 fM) comparable to r-hirudin." @default.
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• W2014128212 date "2003-03-01" @default.
• W2014128212 modified "2023-09-30" @default.
• W2014128212 title "Cloning, purification and biochemical characterization of dipetarudin, a new chimeric thrombin inhibitor" @default.
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• W2014128212 doi "https://doi.org/10.1016/s1570-0232(02)00739-0" @default.
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