{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,19]],"date-time":"2025-10-19T15:33:02Z","timestamp":1760887982297},"reference-count":24,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2006,10,19]],"date-time":"2006-10-19T00:00:00Z","timestamp":1161216000000},"content-version":"vor","delay-in-days":5039,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Nahrung"],"published-print":{"date-parts":[[1993,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Selected physico\u2010chemical properties of pea legumin before and after succinylation have been investigated using isoelectric focusing, PAGE, SDS\u2010PAGE, hydrophobicity measurements, SE\u2010HPLC and RP\u2010HPLC.<\/jats:p><jats:p>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\u2010HPLC. The results of SDS\u2010PAGE provided evidence for the exposure of \u03b1\u2010polypeptide chains in the native legumin.<\/jats:p><jats:p>High succinylation resulted in a decrease of the surface hydrophobicity (<jats:italic>S<\/jats:italic><jats:sub>0<\/jats:sub>) measured by both fluorescence probes (cis\u2010parinaric acid and anilino\u2010naphtalene sulfonic acid). RP\u2010HPLC gave a response both to conformational changes and the introduced succinyl residues.<\/jats:p>","DOI":"10.1002\/food.19930370602","type":"journal-article","created":{"date-parts":[[2006,11,2]],"date-time":"2006-11-02T21:15:44Z","timestamp":1162502144000},"page":"519-527","source":"Crossref","is-referenced-by-count":6,"title":["Selected physico\u2010chemical properties of succinylated legumin from pea (<i>Pisum sativum<\/i> L.)"],"prefix":"10.1002","volume":"37","author":[{"given":"K. 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