The purification and characterization of a third storage protein (convicilin) from the seeds of pea (<i>Pisum sativum</i> L.)

Croy, R. R. D.; Gatehouse, John A.; Tyler, M.; Boulter, D.

doi:10.1042/bj1910509

Cited by 143 publications

(91 citation statements)

References 16 publications

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“…4) which show convicilin patterns similar to those of lines 1238 and 1263 respectively. Since convicilin is a storage protein distinct from the rest of the vicilin fraction (Croy et a!., 1980c), the VA designation for this locus is clearly invalid. The other vicilin loci identified by Thomson and Schroeder (VB, VC) were not considered in this study.…”

Section: Discussionmentioning

confidence: 99%

“…50,000 Mr subunits as synthesised, some of which are subsequently proteolytically cleaved to generate polypeptides of smaller Mr (Croy et al, 1980b; Gatehouse et al, 1981); and thirdly, convicilin, a protein of Mr 280,000 containing only subunits of approx. 70,000 Mr (Croy et a!., 1980c), which do not appear to undergo extensive post-translational modification.…”

Section: Introductionmentioning

confidence: 99%

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Inheritance and mapping of storage protein genes in Pisum sativum L.

Matta

Gatehouse

1982

Heredity

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SUMMARYOne and two-dimensional sodium dodecyl sulphate polyacrylamide gel electrophoretic techniques have been used to follow the inheritance of legumin and convicilin subunits in crosses of various pea lines. The major legumin acidic subunits behaved as products of a single Mendelian gene with at least five different possible alleles. Independent segregation of a minor "big" legumin acidic subunit and the acidic and basic subunits of "small" legumin were observed, suggesting that while the main legumin subunits are produced from a set of closely linked genes at a single locus, further weakly expressed legumin genes are present at other loci. Convicilin subunits behaved as the products of a single Mendelian gene with at least three allelic forms. Genetic analysis of F2 seeds and plants from crosses of pea lines was used to map the major legumin gene (Lg-1) to a locus near the r-tl segment of chromosome 7 and the convicilin gene (Cvc) to a locus between s and k on chromosome 2.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Inheritance and mapping of storage protein genes in Pisum sativum L.

Matta

Gatehouse

1982

Heredity

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“…This is unusual, since no posttranslational modification other than signal peptide cleavage has been reported for convicilins (Croy et al, 1980;Newbigin et al, 1990). Degradation during extraction cannot be excluded; therefore, processing of LCP1 and LCP2 needs further investigation.…”

Section: Globulin Seed Storage Proteins and Globulin Genes In Lotusmentioning

confidence: 99%

The Proteome of Seed Development in the Model Legume Lotus japonicus

et al. 2009

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We have characterized the development of seeds in the model legume Lotus japonicus. Like soybean (Glycine max) and pea (Pisum sativum), Lotus develops straight seed pods and each pod contains approximately 20 seeds that reach maturity within 40 days. Histological sections show the characteristic three developmental phases of legume seeds and the presence of embryo, endosperm, and seed coat in desiccated seeds. Furthermore, protein, oil, starch, phytic acid, and ash contents were determined, and this indicates that the composition of mature Lotus seed is more similar to soybean than to pea. In a first attempt to determine the seed proteome, both a two-dimensional polyacrylamide gel electrophoresis approach and a gel-based liquid chromatography-mass spectrometry approach were used. Globulins were analyzed by two-dimensional polyacrylamide gel electrophoresis, and five legumins, LLP1 to LLP5, and two convicilins, LCP1 and LCP2, were identified by matrix-assisted laser desorption ionization quadrupole/time-of-flight mass spectrometry. For two distinct developmental phases, seed filling and desiccation, a gel-based liquid chromatography-mass spectrometry approach was used, and 665 and 181 unique proteins corresponding to gene accession numbers were identified for the two phases, respectively. All of the proteome data, including the experimental data and mass spectrometry spectra peaks, were collected in a database that is available to the scientific community via a Web interface (http://www.cbs.dtu.dk/cgi-bin/lotus/db.cgi). This database establishes the basis for relating physiology, biochemistry, and regulation of seed development in Lotus. Together with a new Web interface (http:// bioinfoserver.rsbs.anu.edu.au/utils/PathExpress4legumes/) collecting all protein identifications for Lotus, Medicago, and soybean seed proteomes, this database is a valuable resource for comparative seed proteomics and pathway analysis within and beyond the legume family.

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“…The AA profiles of these protein fractions vary considerably among pea cultivars (Gueguen and Barbot 1988), which may explain the variations in AA concentrations observed in the present study. High concentration of lysine and low concentration of TSAA in peas are often attributed to the AA com- position of globulins, vicilin and legumin, which contribute more than 80% of the total seed proteins in peas and are high in lysine but low in TSAA (Croy et al 1980). In the context of meeting the dietary requirement of indispensable AAs for poultry (NRC 1994), cereal grains, canola meal and peas are nutritionally complementary, in that those AAs deficient in one (lysine in cereals and canola and sulphur AAs in peas) are adequate in the other.…”

Section: Composition Of the Pea Cultivarsmentioning

confidence: 99%

Field peas: Chemical composition and energy and amino acid availabilities for poultry

Igbasan¹,

Guenter²,

Slominski³

1997

Can. J. Anim. Sci.

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Field peas: Chemical composition and energy and amino acid availabilities for poultry. Can. J. Anim. Sci. 77: 293-300. Twelve pea cultivars (yellow-, green-and brown-seeded) were evaluated for chemical composition and digestibility in poultry. The evaluation involved analyses for protein, amino acids (AAs), fat, starch, dietary fibre, ash, calcium, phosphorus and tannins. True metabolizable energy [nitrogen corrected (TME n ) and uncorrected (TME)] and true AA bioavailability values were also determined with adult cockerels. The cultivars showed a wide range of protein (207.5-264.0 g kg -1 ) and starch (385.3-436.8 g kg -1 ) contents which were not related to the seed coat colours. The concentrations of several AAs varied among the cultivars. With the exception of arginine, the concentrations of all other essential AAs on a protein basis decreased as protein levels increased. Out of 10 essential AAs including cystine, only arginine had a positive correlation (r = 0.79) with protein content. The dietary fibre contents varied between 190.7 and 223.1 g kg -1 and the values were slightly higher in the brown-seeded cultivars. The brown-seeded cultivars contained appreciable quantities of tannins, while the yellow-and green-seeded cultivars were devoid of tannins. The cultivars were almost devoid of fat and calcium but relatively high in phosphorus. Starch and dietary fibre were negatively correlated with protein content (r = -0.78 and -0.46, respectively), and accounted for the greatest difference in protein content. The TME values ranged from 11.6 to 13.3 MJ kg -1 while the TME n values ranged from 11.0 to 12.9 MJ kg -1 . The mean availabilities of AAs ranged from a high of 89.6 to a low of 75.9%, with total sulphur AAs (cystine and methionine) having the lowest value and glutamic acid having the highest value. There was a trend (P ≤ 0.05) towards lower AA bioavailability values in the brown-seeded cultivars. It can be concluded that these cultivars varied in chemical composition, metabolizable energy content and bioavailability of AAs.Key words: Field peas, composition, digestibility, chicken, poultry Igbasan, F. A., Guenter, W. et Slominski, B. A. 1997. Pois de grande culture : composition chimique et disponibilité de l'én-ergie et des acides aminés pour la volaille. Can. J. Anim. Sci. 77: 293-300. Douze cultivars de pois à grain jaune, vert et brun ont été évalués sur la composition chimique et sur la digestibilité chez les volailles. L'évaluation comportait les analyses des teneurs en protéine, en acides aminés (AA), en matière grasse, en amidon, en fibres, en cendres, en calcium, en phosphore et en tanins. L'énergie métabolisable vraie, corrigée (EMV n ) ou non (EMV) en fonction de la concentration azotée et la biodisponibilité vraie des AA étaient également calculées sur des coqs adultes. On relevait parmi les cultivars un large écart de teneurs en protéine (207,5-264,0 g kg -1 ) et en amidon (385,3-436,8 g kg -1 ), lesquelles n'etaient aucunement reliées à la coloration du tégument. Les concentrations de plu...

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The purification and characterization of a third storage protein (convicilin) from the seeds of pea (Pisum sativum L.)

Cited by 143 publications

References 16 publications

Inheritance and mapping of storage protein genes in Pisum sativum L.

Inheritance and mapping of storage protein genes in Pisum sativum L.

The Proteome of Seed Development in the Model Legume Lotus japonicus

Field peas: Chemical composition and energy and amino acid availabilities for poultry

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