Structural Changes of Legumin from Faba Beans (Vicia faba L.) by Succinylation

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...

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Veröffentlicht in:Journal of agricultural and food chemistry 1998-06, Vol.46 (6), p.2080-2086
Hauptverfasser: Schwenke, Klaus Dieter, Knopfe, Constanze, Mikheeva, Larissa M, Grinberg, Valerij Y
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container_end_page 2086
container_issue 6
container_start_page 2080
container_title Journal of agricultural and food chemistry
container_volume 46
creator Schwenke, Klaus Dieter
Knopfe, Constanze
Mikheeva, Larissa M
Grinberg, Valerij Y
description 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
doi_str_mv 10.1021/jf970984k
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Agric. Food Chem</addtitle><date>1998-06-01</date><risdate>1998</risdate><volume>46</volume><issue>6</issue><spage>2080</spage><epage>2086</epage><pages>2080-2086</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><abstract>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</abstract><pub>American Chemical Society</pub><doi>10.1021/jf970984k</doi><tpages>7</tpages></addata></record>
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ispartof Journal of agricultural and food chemistry, 1998-06, Vol.46 (6), p.2080-2086
issn 0021-8561
1520-5118
language eng
recordid cdi_crossref_primary_10_1021_jf970984k
source ACS Publications
subjects ANALYTICAL METHODS
CHEMICAL COMPOSITION
CHEMICAL REACTIONS
CHEMICAL STRUCTURE
COMPOSICION QUIMICA
COMPOSITION CHIMIQUE
ESTABILIDAD
ESTRUCTURA QUIMICA
FABA BEANS
FEVE
GLOBULINAS
GLOBULINE
GLOBULINS
HABA
HIDROFOBICIDAD
HYDROPHOBICITE
HYDROPHOBICITY
MOLECULAR CONFORMATION
REACCIONES QUIMICAS
REACTION CHIMIQUE
STABILITE
STABILITY
STRUCTURE CHIMIQUE
SUCCINIC ANHYDRIDE
TECHNIQUE ANALYTIQUE
TECNICAS ANALITICAS
VISCOSIDAD
VISCOSITE
VISCOSITY
title Structural Changes of Legumin from Faba Beans (Vicia faba L.) by Succinylation
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