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Specific subunit pairs of legumin from Vicia faba

✍ Scribed by Christian Horstmann

Publisher
Elsevier Science
Year
1983
Tongue
English
Weight
592 KB
Volume
22
Category
Article
ISSN
0031-9422

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πŸ“œ SIMILAR VOLUMES

Limited tryptic hydrolysis of legumin fr
Limited tryptic hydrolysis of legumin from faba bean (Vicia faba L.): formation of an [unequal] subunit pattern
✍ Dudek, Steffi ;Horstmann, Ch. ;Schwenke, K. D. πŸ“‚ Article πŸ“… 1996 πŸ› John Wiley and Sons 🌐 English βš– 742 KB

## 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

Subunit structure of Vicia faba legumin
Subunit structure of Vicia faba legumin and implications for the improvement of protein quality
✍ Horstmann, C. ;MΓΌntz, K. πŸ“‚ Article πŸ“… 1986 πŸ› John Wiley and Sons 🌐 English βš– 567 KB

Legumin, the main storage protein of Viria faba seeds. consists of the two different subunit types A and B. Each subunit is composed of two polypeptide chains, one acidic (2) and one basic (p) linked by disulphide bridges. In each subunit type specific a-P-pairs occur. in type A 3-as well as 8-poly

Changes in interfacial properties of leg
Changes in interfacial properties of legumin from faba beans (Vicia faba I.) by tryptic hydrolysis
✍ Krause, J.-P. ;Schwenke, K. D. πŸ“‚ Article πŸ“… 1995 πŸ› John Wiley and Sons 🌐 English βš– 589 KB

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