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Homology of basic subunits of legumin from Glycine max and Vicia faba

โœ Scribed by J. Gilroy; D. Wright; D. Boulter

Publisher
Elsevier Science
Year
1979
Tongue
English
Weight
212 KB
Volume
18
Category
Article
ISSN
0031-9422

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๐Ÿ“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
โœ Dudek, Steffi ;Horstmann, Ch. ;Schwenke, K. D. ๐Ÿ“‚ Article ๐Ÿ“… 1996 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 742 KB

## Abstract Oneโ€dimensional and twoโ€dimensional SDSโ€PAGE and Hydrophobic Cluster Analysis (HCA) were used for investigating the course of limited tryptic hydrolysis of faba bean legumin. SDSโ€PAGE revealed the formation of an โ€œunequalโ€ subunit pattern, characterized by 30 and 50 kDa subunits, which

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Subunit structure of Vicia faba legumin and implications for the improvement of protein quality
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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
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โœ Krause, J.-P. ;Schwenke, K. D. ๐Ÿ“‚ Article ๐Ÿ“… 1995 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 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