scholarly journals Erratum: A PQL (protein quantity loci) analysis of mature pea seed proteins identifies loci determining seed protein composition

PROTEOMICS ◽  
2011 ◽  
Vol 11 (19) ◽  
pp. 3942-3942 ◽  
Author(s):  
Michael Bourgeois ◽  
Françoise Jacquin ◽  
Florence Cassecuelle ◽  
Vincent Savois ◽  
Maya Belghazi ◽  
...  
Keyword(s):  
Seed Protein ◽  
Seed Proteins ◽  
Protein Composition ◽  
Pea Seed

A PQL (protein quantity loci) analysis of mature pea seed proteins identifies loci determining seed protein composition

PROTEOMICS ◽  
2011 ◽  
Vol 11 (9) ◽  
pp. 1581-1594 ◽  
Author(s):  
Michael Bourgeois ◽  
Françoise Jacquin ◽  
Florence Cassecuelle ◽  
Vincent Savois ◽  
Maya Belghazi ◽  
...  
Keyword(s):  
Seed Protein ◽  
Seed Proteins ◽  
Protein Composition ◽  
Pea Seed

Differences in the seed protein composition of genus Arachis

1984 ◽  
Vol 62 (1) ◽  
pp. 105-108 ◽  
Author(s):  
Sheikh M. Basha ◽  
Sunil K. Pancholy
Keyword(s):  
Seed Protein ◽  
Leucine Aminopeptidase ◽  
Gel Filtration ◽  
Seed Proteins ◽  
Protein Composition ◽  
The Other ◽  
Total Amino Acid ◽  
Arachis Species ◽  
High Molecular Weight Proteins ◽  
Column Comparison

Seed proteins from various Arachis species were extracted and fractionated by gel filtration on a Sephacryl S-300 column. Comparison of the protein profiles revealed the presence of wide variations in their protein composition. Major differences were observed in the amounts of methionine-rich proteins, arachin, and the high molecular weight proteins among the various species. Additionally, differences in the total amino acid composition (histidine, threonine, proline, glycine, cystine, valine, methionine, and tyrosine) were also detected. The defatted meals of the nonnodulating line contained the lowest amount (36%) of protein, while the other species ranged between 49 and 57%. Leucine aminopeptidase and acid phosphatase activities were highest in Arachis villosulicarpa and lowest in Arachis monticola.

scholarly journals Variability in Protein Composition of Pea Seed Studied by FPLC and Multidimensional Analysis

Crop Science ◽  
1998 ◽  
Vol 38 (6) ◽  
pp. 1568-1575 ◽  
Author(s):  
A. Baniel ◽  
D. Bertrand ◽  
A. Lelion ◽  
J. Guéguen
Keyword(s):  
Protein Composition ◽  
Multidimensional Analysis ◽  
Pea Seed

Electropherogram pattern similarity of seed proteins from 21 different soybean (Glycine max) varieties

1977 ◽  
Vol 55 (16) ◽  
pp. 2245-2250 ◽  
Author(s):  
Clifton F. Savoy
Keyword(s):  
Glycine Max ◽  
Seed Protein ◽  
Sodium Dodecyl ◽  
Seed Proteins ◽  
Plant Proteins ◽  
Relative Mobility ◽  
Molecular Weights ◽  
Pattern Similarity ◽  
Protein Components ◽  
Phosphate Detergent

Soybean (Glycine max) seed protein has been characterized using a phosphate-detergent (sodium dodecyl sulfate) polyacrylamide gel electrophoretic system, which has been extensively tested on plant proteins. The same general densitometer electropherogram pattern as regards numbers and kinds of protein components resolved was observed for all soybean varieties tested, and one pattern is presented along with appropriate descriptive characterizations (numbers, molecular weights, relative mobility, and light absorption at 597 nm) to aid in distinguishing the components. Quantitative differences, however, of individual components may occur.

Taxonomic significance of seed protein profiles in Acacia, with special reference to Acacia emilioana

2003 ◽  
Vol 16 (1) ◽  
pp. 35 ◽  
Author(s):  
Alicia L. Lamarque ◽  
Renée H. Fortunato
Keyword(s):  
Seed Protein ◽  
Seed Proteins ◽  
High Concentration ◽  
Protein Patterns ◽  
Qualitative And Quantitative ◽  
Sds Page ◽  
Electrophoretic Data ◽  
Main Protein ◽  
Protein Components ◽  
Total Seed

Total seed proteins of 10 Acacia species were examined by SDS–PAGE. The protein patterns showed qualitative and quantitative differences among the taxa analysed. The main protein components of most species examined had MW's in the range of 38.5–49.0 × 103. Subgenus Aculeiferum differed from subg. Acacia in the presence of a high concentration of proteins in the range of 20–24.5 × 103. Hierarchical clustering of the 10 taxa was undertaken, based on Jaccard distances calculated from electrophoretic data. The species grouped in two main clusters, representing the two subgenera of Acacia that occur in America, namely subg. Acacia and subg. Aculeiferum. The taxonomic placement of Acacia emilioana, a species with uncertain sectional affinity within subg. Aculeiferum, is discussed.

The systematic position of the genus Rhinanthus (Scrophulariaceae) in North America

1986 ◽  
Vol 64 (7) ◽  
pp. 1443-1449 ◽  
Author(s):  
Robert van Hulst ◽  
Andrée Thériault ◽  
Bill Shipley
Keyword(s):  
North American ◽  
Seed Protein ◽  
Seed Proteins ◽  
Great Majority ◽  
Morphological Characters ◽  
Systematic Position ◽  
Seed Morphology ◽  
Species Level ◽  
General Morphology ◽  
Interpopulation Variation

North American plants of the genus Rhinanthus are generally designated as R. crista-galli L., or sometimes as R. borealis (Sterneck) Druce or R. stenophyllus (Schur) Druce. The name R. crista-galli, however, has been declared a nomen dubium, and in Europe the corresponding plant is now known as R. minor L. We have compared North American and European material of Rhinanthus on the basis of general morphology, soluble seed proteins, and seed morphology. General morphology proved to be a poor guide to interpopulation variation in these highly plastic plants, even when aided by numerical methods. Seed protein banding has already been shown to be an extremely valuable and stable guide to taxonomy at or below the species level. We have demonstrated four distinct protein banding types in our material: a southeastern Canadian type (S), a northern Canadian type (N), a European type (E), and a hybrid between S and N. Subsequently, we have attempted to allocate populations to the correct seed protein type on the basis of seed morphology alone using discriminant analysis. This allocation is correct in the great majority of cases. We propose that both the southern Canadian and European types be designated as R. minor var. minor (although the two types can in some cases be distinguished on the basis of seed proteins), and that the northern Canadian type be called R. minor var. borealis. We also present a survey of the seed morphological characters that serves to distinguish the two varieties.

Genetic diversity for seed protein composition in Medicago truncatula

2005 ◽  
Vol 3 (1) ◽  
pp. 59-71 ◽  
Author(s):  
C. Le Signor ◽  
K. Gallardo ◽  
J.M. Prosperi ◽  
C. Salon ◽  
L. Quillien ◽  
...  
Keyword(s):  
Protein Content ◽  
Medicago Truncatula ◽  
Seed Protein ◽  
Geographical Origin ◽  
Protein Composition ◽  
Seed Protein Content ◽  
Genetic Determination ◽  
One Dimensional ◽  
Autogamous Species ◽  
Protein Classes

Fifty lines of Medicago truncatula, derived from ecotypes or cultivars of diverse geographical origin, were grown under uniform conditions, and variation in seed protein composition and quantity was investigated. One-dimensional electrophoretic profiles revealed 46 major seed polypeptides, of which 26 were polymorphic within the collection. The vicilin/convicilin (7S) and the legumin (11S) type proteins were identified by immunoblotting using antibodies raised against the homologous pea proteins. The polymorphism for the major seed protein classes allowed the clustering of the genotypes into four groups. There was no evidence of clustering according to geographical origin of the lines. However, all lines not belonging to either M. truncatula ssp. truncatula or ssp. longispina were clustered in a single group, demonstrating the value of seed protein profiles in delimiting species boundaries. The Jemalong line group was differentiated early in the dendrogram, and thus represents an ancient clade in the seed diversity of M. truncatula. Within-accession variation was investigated for one-dimensional seed profiles, with additional lines obtained from the same ecotypes. As expected for an autogamous species, within-accession variation was low. Seed protein content was highly variable among the 50 lines examined. Lines contrasting for qualitative traits and seed protein content were identified to allow for the genetic determination of these characters.

DISCRIMINATION OF CULTIVARS OF LENTIL (Lens culinaris Medic.) BY ELECTROPHORESIS OF SEED PROTEINS

1989 ◽  
Vol 69 (1) ◽  
pp. 243-246 ◽  
Author(s):  
A. HUSSAIN ◽  
W. BUSHUK ◽  
K. W. CLARK
Keyword(s):  
Gel Electrophoresis ◽  
Lens Culinaris ◽  
Seed Protein ◽  
Cultivar Identification ◽  
Polyacrylamide Gel Electrophoresis ◽  
Seed Proteins ◽  
Polyacrylamide Gel

Discrimination of lentil cultivars was achieved by analysis of seed protein by two types of polyacrylamide gel electrophoresis. Cultivars of lentil were discriminated by the presence or absence of diagnostic bands. Electrophoregrams of six seed lots of the cultivar Eston were identical and unaffected by growing conditions.Key words: Lens culinaris Medic, seed proteins, polyacrylamide gel electrophoresis, cultivar identification

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