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Time-resolved Tryptophan Fluorescence of Fragment 1-86 of Factor X and the Influence of Membrane Binding

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    0181508 - UFCH-W 20020246 RIV CZ eng J - Journal Article
    Häfner, A. - Mérola, F. - Duportail, G. - Schneider, F. W. - Hof, Martin - Beneš, Martin
    Time-resolved Tryptophan Fluorescence of Fragment 1-86 of Factor X and the Influence of Membrane Binding.
    Collection of Czechoslovak Chemical Communications. Roč. 67, - (2002), s. 1872-1882. ISSN 0010-0765
    R&D Projects: GA MŠMT LN00A032
    Institutional research plan: CEZ:AV0Z4040901
    Keywords : protein fluorescence * factor Xa * Gla domain
    Subject RIV: CF - Physical ; Theoretical Chemistry
    Impact factor: 0.848, year: 2002

    Membrane binding of the N-terminus of the prothrombinase reaction enzyme, fragment 1-86 of factor X, to phospholipid vesicles was studied using time-resolved fluorescence spectroscopy of the tryptophan residue Trp41 which is located in the membrane binding part of this protein (Gla domain). Fluorescence lifetimes were determined by the time-correlated single photon couting technique using synchrotron radiation as the excitation source.
    Permanent Link: http://hdl.handle.net/11104/0078067


     
     

Number of the records: 1  

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