Document Detail

Selected physico-chemical properties of succinylated legumin from pea (Pisum sativum L.).
MedLine Citation:
PMID:  8121465     Owner:  NLM     Status:  MEDLINE    
Selected physico-chemical properties of pea legumin before and after succinylation have been investigated using isoelectric focusing, PAGE, SDS-PAGE, hydrophobicity measurements, SE-HPLC and RP-HPLC. Exhaustive succinylation shifted the I.P. of legumin from 4.75 to 3.5. The stepwise dissociation of legumin by increasing succinylation has been confirmed both by means of PAGE in a nondenaturing system, and by SE-HPLC. The results of SDS-PAGE provided evidence for the exposure of alpha-polypeptide chains in the native legumin. High succinylation resulted in a decrease of the surface hydrophobicity (S0) measured by both fluorescence probes (cis-parinaric acid and anilino-naphthalene sulfonic acid). RP-HPLC gave a response both to conformational changes and the introduced succinyl residues.
K D Schwenke; R Mothes; B Raab; H Rawel; J Gueguen
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Die Nahrung     Volume:  37     ISSN:  0027-769X     ISO Abbreviation:  Nahrung     Publication Date:  1993  
Date Detail:
Created Date:  1994-04-04     Completed Date:  1994-04-04     Revised Date:  2009-11-11    
Medline Journal Info:
Nlm Unique ID:  0142530     Medline TA:  Nahrung     Country:  GERMANY    
Other Details:
Languages:  eng     Pagination:  519-27     Citation Subset:  IM    
Forschungsgruppe Pflanzenproteinchemie (WIP), Universität Potsdam, Federal Republic of Germany.
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MeSH Terms
Chromatography, High Pressure Liquid
Electrophoresis, Polyacrylamide Gel
Fabaceae / chemistry*
Isoelectric Focusing
Plant Proteins / chemistry*
Plants, Medicinal*
Protein Conformation
Succinates / chemistry*
Surface Properties
Reg. No./Substance:
0/Plant Proteins; 0/Succinates; 0/legumin protein, plant

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