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Structural Changes of Legumin from Faba Beans (Vicia faba L.) by Succinylation
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    Structural Changes of Legumin from Faba Beans (Vicia faba L.) by Succinylation
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    University Potsdam, WIP-Forschungsgruppe Pflanzenproteinchemie, Arthur-Scheunert-Allee 114-116, D-14558 Bergholz-Rehbrücke, Germany, and Russian Academy of Sciences, Institute of Biochemical Physics, Vavilow Street 28, Moscow, Russia
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    Journal of Agricultural and Food Chemistry

    Cite this: J. Agric. Food Chem. 1998, 46, 6, 2080–2086
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    https://doi.org/10.1021/jf970984k
    Published May 1, 1998
    Copyright © 1998 American Chemical Society

    Abstract

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    The effect of progressive succinylation upon the conformation of faba bean legumin has been studied using chemical analysis, viscometry, analytical ultracentrifugation, UV and fluorescence spectroscopy, and differential scanning calorimetry (DSC). The protein dissociates gradually into 3 S subunits forming a 7 S intermediate. DSC measurements revealed a continuous loosening of the spacial structure with increasing degree of succinylation. Viscometric and spectroscopic studies indicate the presence of a particular conformational state at 60−80% succinylation, whereas a largely expanded structure was shown to exist in exhaustively succinylated legumin due to a cumulative effect of N- and O-succinylation.

    Keywords: Legumin; faba bean protein; succinylation; conformational changes

    Copyright © 1998 American Chemical Society

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     Corresponding author's present address:  Institut für Angewandte Proteinchemie e.V., Stahnsdorfer Damm 81, D-14532 Kleinmachnow, Germany (e-mail food.proteins@ prochem.pm.shuttle.de).

     University Potsdam.

     Russian Academy of Sciences.

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    Journal of Agricultural and Food Chemistry

    Cite this: J. Agric. Food Chem. 1998, 46, 6, 2080–2086
    Click to copy citationCitation copied!
    https://doi.org/10.1021/jf970984k
    Published May 1, 1998
    Copyright © 1998 American Chemical Society

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