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Physical adsorption of human thrombomodulin (ART-123) onto polymeric biomaterials for developing an antithrombogenic blood-contacting material.

Physical adsorption of human thrombomodulin (ART-123) onto polymeric biomaterials for developing an antithrombogenic blood-contacting material. Research Abstract Details 

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  • Physical adsorption of human thrombomodulin (ART-123) onto polymeric biomaterials for developing an antithrombogenic blood-contacting material. Abstract Text:

    michiya matsusakiMichiya Matsusaki,masaaki omichiMasaaki Omichi,ikuro maruyamaIkuro Maruyama,mitsuru akashiMitsuru Akashi,michiya matsusakiMichiya Matsusaki,masaaki omichiMasaaki Omichi,ikuro maruyamaIkuro Maruyama,mitsuru akashiMitsuru Akashi,michiya matsusakiMichiya Matsusaki,masaaki omichiMasaaki Omichi,ikuro maruyamaIkuro Maruyama,mitsuru akashiMitsuru Akashi,

    Human thrombomodulin (hTM) is an endothelial cell-associated protein with potent natural anticoagulant activity by converting thrombin from a procoagulant protease to an anticoagulant. ART-123 is a recombinant soluble hTM (amino acid residues 1-498), and we focused on the physical adsorption of ART-123 onto a polymeric biomaterial surface to develop an antithrombogenic blood-contacting material with preventing the denaturation of hTM and the remaining chemical reagents. The adsorption of hTM onto polysulfone (PSF) films was analyzed quantitatively by quartz crystal microbalance analysis. The adsorption constant and the maximum adsorption amount, calculated by the assumption of a Langmuir-type adsorption, showed that hTM adsorbed with a relatively weak interaction onto the PSF film. The hydrophilic protein lysozyme also showed a Langmuir-type monolayer adsorption, although hydrophobic catalase and fibrinogen showed multilayer adsorption accompanying the denaturation. The physically adsorbed hTM showed high coenzymatic activity for the activation of protein C, as well as anticoagulant activity. Furthermore, the surface wettability of the PSF film was easily controllable by the physical adsorption of hydrophobic and hydrophilic bioactive proteins. The physical adsorption of hTM or bioactive proteins onto polymeric biomaterials will be instrumental for developing an antithrombogenic blood-contacting biomaterial, and for controlling the surface properties of biomaterials. (c) 2007 Wiley Periodicals, Inc. J Biomed Mater Res, 2008.

    Physical adsorption of human thrombomodulin (ART-123) onto polymeric biomaterials for developing an antithrombogenic blood-contacting material. Publishing Authors By Initials

    m matsusakiM Matsusaki,m omichiM Omichi,i maruyamaI Maruyama,m akashiM Akashi,m matsusakiM Matsusaki,m omichiM Omichi,i maruyamaI Maruyama,m akashiM Akashi,m matsusakiM Matsusaki,m omichiM Omichi,i maruyamaI Maruyama,m akashiM Akashi,

    For similar abstracts research abstracts see: abstracts research

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    Physical adsorption of human thrombomodulin (ART-123) onto polymeric biomaterials for developing an antithrombogenic blood-contacting material. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: Journal of biomedical materials research. Part A

    VOLUME: 84

    Page Numbers: 1-9

    Journal Abbreviation:

    ISSN: 1549-3296

    DAY: 26

    MONTH: Jan

    YEAR: 2008

    Physical adsorption of human thrombomodulin (ART-123) onto polymeric biomaterials for developing an antithrombogenic blood-contacting material. Information

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    LANGUAGE: eng

    NlmUniqueID: 101234237

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    Grant and Affiliation Information for Physical adsorption of human thrombomodulin (ART-123) onto polymeric biomaterials for developing an antithrombogenic blood-contacting material.

    AFFILIATION: Department of Applied Chemistry, Graduate School of Engineering, Osaka University, 2-1 Yamada-Oka, Suita 565-0871, Japan.

    Country: United States

    United States Research PublicationUnited States Research Publication

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    MEDLINETA: J Biomed Mater Res A

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