| Selected physico-chemical properties of succinylated legumin from pea (Pisum sativum L.). | |
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MedLine Citation:
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PMID: 8121465 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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K D Schwenke; R Mothes; B Raab; H Rawel; J Gueguen |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Die Nahrung Volume: 37 ISSN: 0027-769X ISO Abbreviation: Nahrung Publication Date: 1993 |
Date Detail:
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Created Date: 1994-04-04 Completed Date: 1994-04-04 Revised Date: 2009-11-11 |
Medline Journal Info:
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Nlm Unique ID: 0142530 Medline TA: Nahrung Country: GERMANY |
Other Details:
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Languages: eng Pagination: 519-27 Citation Subset: IM |
Affiliation:
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Forschungsgruppe Pflanzenproteinchemie (WIP), Universität Potsdam, Federal Republic of Germany. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Chromatography, High Pressure Liquid Electrophoresis, Polyacrylamide Gel Fabaceae / chemistry* Isoelectric Focusing Plant Proteins / chemistry* Plants, Medicinal* Protein Conformation Succinates / chemistry* Surface Properties |
| Chemical | |
Reg. No./Substance:
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0/Plant Proteins; 0/Succinates; 0/legumin protein, plant |
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