title: Selected physico-chemical properties of succinylated legumin from pea (Pisum sativum L.).
abstract: 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.
authors.affiliation: Forschungsgruppe Pflanzenproteinchemie (WIP), Universität Potsdam, Federal Republic of Germany.
authors.forename: K D
authors.initials: KD
authors.lastname: Schwenke
authors.forename: R
authors.initials: R
authors.lastname: Mothes
authors.forename: B
authors.initials: B
authors.lastname: Raab
authors.forename: H
authors.initials: H
authors.lastname: Rawel
authors.forename: J
authors.initials: J
authors.lastname: Gueguen
mesh_terms: D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D007887:Fabaceae / Q000737:chemistry*; D007525:Isoelectric Focusing; D010940:Plant Proteins / Q000737:chemistry*; D010946:Plants, Medicinal; D011487:Protein Conformation; D013386:Succinates / Q000737:chemistry*; D013499:Surface Properties; D000097793:Legumins
chemical_list: D010940:Plant Proteins; D013386:Succinates; D000097793:Legumins