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• W2031574013 abstract "Anticoagulation factor I (ACF I) from the venom of Agkistrodon acutus is a binding protein to activated coagulation factor X (FXa) and possesses marked anticoagulant activity. Single ACF I molecule has been successfully imaged in air by tapping mode atomic force microscopy (AFM) with high-resolution using glutaraldehyde as a coupling agent. The physical adsorption and covalent binding of ACF I onto the mica show very different surface topographies. The former exhibits the characteristic strand-like structure with much less reproducibility, the latter displays a elliptic granular structure with better reproducibility, which suggests that the stability of ACF I molecules on the mica is enhanced by covalent bonding in the presence of glutaraldehyde. A small-scale AFM amplitude-mode image clearly shows that the covalently bonded ACF I molecule by glutaraldehyde has olive shape structure with an average size of 7.4 nm × 3.6 nm × 3.1 nm, which is very similar to the size determined from the crystal structure of ACF I." @default.
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• W2031574013 date "2010-08-26" @default.
• W2031574013 modified "2023-09-22" @default.
• W2031574013 title "Single-Molecular Imaging of Anticoagulation Factor I from Snake Venom by Atomic Force Microscopy" @default.
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• W2031574013 doi "https://doi.org/10.1002/cjoc.20020200919" @default.
• W2031574013 hasPublicationYear "2010" @default.
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