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

✍ Scribed by Schwenke, Klaus Dieter; Knopfe, Constanze; Mikheeva, Larissa M.; Grinberg, Valerij Y.


Book ID
127199381
Publisher
American Chemical Society
Year
1998
Tongue
English
Weight
107 KB
Volume
46
Category
Article
ISSN
0021-8561

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Changes of the surfxe tension at a planar interface and of the emulsifying properties of tryptically digested legumin from faba beans (enzyme/substrate ratio = 1/40) were studied in terms of time of hydrolysis (0-48 h). Simultaneously, molecular changes of legumin were studied by determination of li

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## Abstract One‐dimensional and two‐dimensional SDS‐PAGE and Hydrophobic Cluster Analysis (HCA) were used for investigating the course of limited tryptic hydrolysis of faba bean legumin. SDS‐PAGE revealed the formation of an β€œunequal” subunit pattern, characterized by 30 and 50 kDa subunits, which