Investigations of Vicilin and Legumin.

Danielsson, Carl-Erik; Willstaedt, Ebba; Lund, L. Koren; Hakala, Maire

doi:10.3891/acta.chem.scand.03-0041

Cited by 15 publications

(1 citation statement)

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“…Further detailed information has been given by Danielsson (1949aDanielsson ( , b, 1952; Derbyshire et al (1976); Sutcliffe and Pate (1977); Boulter (1979); Casey (1979); Bewley and Black (1979); Millier and Werner (1979); ; Khan et al (1980). In Pisum sativum, the ratio of globulin to albumin is 1: 1.6; 60% of seed proteins are globulins.…”

Section: The Characterization Of Seed Proteinsmentioning

confidence: 99%

Induced Mutations in Plant Breeding

Gottschalk¹,

Wolff²

1983

Monographs on Theoretical and Applied Genetics

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Section: The Characterization Of Seed Proteinsmentioning

confidence: 99%

Induced Mutations in Plant Breeding

Gottschalk¹,

Wolff²

1983

Monographs on Theoretical and Applied Genetics

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Untersuchungen an Samenglobulinen von Leguminosen. 3. Mitt. Über Samenglobuline der Ackerbohne (Vicia faba L.)

Scholz¹,

Manteuffel²

1975

Nahrung

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The seed globulins from Vicia faba predominantly consist of two components, vicilin and legumin, which are exclusively deposited within the protein bodies of the storage cotyledons. The globulin biosynthesis commences with high intensity within a distinct phase during seed development as a consequence of reactivated genetic information. Isolation and purification of vicilin and legumin were achieved by a combination of zone precipitation, ion exchange chromatography, and gel filtration. Purity was controlled by disc electrophoresis on polyacrylamide e gels at pH 4.3 and by two dimensional immunoelectrophoresis, respectively. Vicilin prepared by zone precipitation and ion exchange chromatography consists of several serologically different proteins. One of them occupies the legumin position on polyacrylamide gels, although not identic with legumin, as revealed by tandem immunoelectrophoresis. The serological nonrelationship of vicilin and legumin was confirmed. Vicilin is characterized by micro heterogeneity which seems to indicate a molecular polymorphism.

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Quantitative studies on the cotyledonary proteins in the genus Pisum

Schroeder

1982

J Sci Food Agric

100

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Forty-five lines of peas including primitive or wild forms, field peas, and round and wrinkled garden peas, were grown under uniform conditions and the seeds examined for variation in protein characteristics likely to influence nutritional value. The characters measured were crude protein, extractable protein, globulins and albumins, the percentages of legurnin, total sulphur and protein sulphur, carbon: nitrogen and nitrogen: sulphur ratios. The extractable protein was separated quantitatively into an albumin fraction (20-35 %) and a globulin fraction (legumin and vicilin). Without exception lines high in albumin content were low in legumin content (correlation coefficient r = -0.757). As both the albumin fraction and legumin are rich in sulphur amino acids, this negative correlation has important implications for attempts through plant breeding to improve the nutritional quality of legume seed proteins, by increasing the sulphur amino acid content. Total sulphur was not correlated with any other protein character.

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Investigations of Vicilin and Legumin.

Cited by 15 publications

References 0 publications

Induced Mutations in Plant Breeding

Induced Mutations in Plant Breeding

Untersuchungen an Samenglobulinen von Leguminosen. 3. Mitt. Über Samenglobuline der Ackerbohne (Vicia faba L.)

Quantitative studies on the cotyledonary proteins in the genus Pisum

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