scholarly journals ANALYSIS OF INTROGRESSIVE LINES OF INTER-SPECIES PEA HYBRIDS BY BAND COMPOSITION OF SEED PROTEINS

2020 ◽  
Author(s):  
Sergey Bobkov ◽  
Ivan Bychkov ◽  
Tatyana Selikhova ◽  
Elena Semenova ◽  
Vishnyakova Margarita
Keyword(s):  
Interspecific Hybrids ◽  
Seed Protein ◽  
Storage Proteins ◽  
Seed Proteins ◽  
Protein Isoforms ◽  
Wild Parent ◽  
Polymorphic Position ◽  
Reproductive Incompatibility ◽  
Protein Spectra ◽  
Electrophoretic Spectrum

Background. The reproductive incompatibility of cultivated (Pisum sativum) and wild (P. fulvum) pea species determines the difficulties of obtaining hybrids as well as the transfer of valuable wild parent alleles into interspecific hybrids and their use in the breeding process. The aim of the research was a comparative study of protein spectra of pea interspecific hybrids BC2F5 P. sativum x P. fulvum obtained by the authors and their parents. Materials and methods. The band composition of seed proteins in the interspecific hybrids of peas BC2F5, variety Stabil (P. sativum) accession from VIR collection I-609881 (P. fulvum) has been studied. Effectiveness of parent gene transfer determining each polymorphic position of electrophoretic spectrum were evaluated. Results. The ratio of the actual frequencies of the bands of the cultivated and wild parents in the introgression lines corresponded to the expected level in 73% of the positions of the electrophoretic spectrum. The introgression rate of individual seed protein bands from wild parent into interspecific pea hybrids in the absence of selection significantly exceeded the expected level, which may indicate the adaptive value of alleles encoding unique seed protein isoforms. Conclusion. The possibility of introgressive transfer of wild-type alleles to the cultivated genotypes of pea, as well as the presence of identified cultivated isoforms of storage proteins in all studied lines of BC2F5 interspecific hybrids in 88.2% of the polymorphic positions of the electrophoretic spectrum, indicates the possibility of using the wild species P. fulvum in pea breeding.

scholarly journals A Single Seed Protein Extraction Protocol for Characterizing Brassica Seed Storage Proteins

Agronomy ◽  
2021 ◽  
Vol 11 (1) ◽  
pp. 107
Author(s):  
Mahmudur Rahman ◽  
Lei Liu ◽  
Bronwyn J. Barkla
Keyword(s):  
Seed Protein ◽  
Storage Proteins ◽  
Protein Extraction ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Protein Yield ◽  
Tissue Type ◽  
Single Seed ◽  
Material Optimization ◽  
Hazardous Chemical

Rapeseed oil-extracted expeller cake mostly contains protein. Various approaches have been used to isolate, detect and measure proteins in rapeseeds, with a particular focus on seed storage proteins (SSPs). To maximize the protein yield and minimize hazardous chemical use, isolation costs and the loss of seed material, optimization of the extraction method is pivotal. For some studies, it is also necessary to minimize or avoid seed-to-seed cross-contamination for phenotyping and single-tissue type analysis to know the exact amount of any bioactive component in a single seed, rather than a mixture of multiple seeds. However, a simple and robust method for single rapeseed seed protein extraction (SRPE) is unavailable. To establish a strategy for optimizing SRPE for downstream gel-based protein analysis, yielding the highest amount of SSPs in the most economical and rapid way, a variety of different approaches were tested, including variations to the seed pulverization steps, changes to the compositions of solvents and reagents and adjustments to the protein recovery steps. Following SRPE, 1D-SDS-PAGE was used to assess the quality and amount of proteins extracted. A standardized SRPE procedure was developed and then tested for yield and reproducibility. The highest protein yield and quality were obtained using a ball grinder with stainless steel beads in Safe-Lock microcentrifuge tubes with methanol as the solvent, providing a highly efficient, economic and effective method. The usefulness of this SRPE was validated by applying the procedure to extract protein from different Brassica oilseeds and for screening an ethyl methane sulfonate (EMS) mutant population of Brassica rapa R-0-18. The outcomes provide useful methodology for identifying and characterizing the SSPs in the SRPE.

scholarly journals Genetic Diversity of Common Bean Genotypes as Revealed By Seed Storage Proteins and Some Agronomic Traits

2014 ◽  
Vol 67 (1) ◽  
pp. 125-137 ◽  
Author(s):  
Akbar Marzooghian ◽  
Mohammad Moghaddam ◽  
Mostafa Valizadeh ◽  
Mohammad Hasan Kooshki
Keyword(s):  
Genetic Diversity ◽  
Common Bean ◽  
Yield Components ◽  
Storage Proteins ◽  
Agronomic Traits ◽  
Morphological Characteristics ◽  
Seed Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Seed Morphology

AbstractEvaluation of the genetic diversity present within species is essential for conservation, management and utilization of the genetic resources. The objective of this study was to evaluate genetic variability of 70 common bean genotypes for seed storage proteins, grain morphological characteristics and agronomic traits. Two methods of extracting soluble seed proteins in salt were used.Positive correlations were observed among both seed morphological characters and developmental characters while yield components showed negative correlations with each other. Factor analysis for agronomic and grain morphological traits resulted in three factors were named yield components, seed morphology and phenology, respectively. Most genotypes had lower or medium scores for yield components and phenology factors. Considerable diversity was observed for seed morphology factor among the common bean genotypes.Nei’s diversity coefficient (He= 0.4), effective number of alleles (Ae= 1.69) and number of polymorphic loci (N = 17) indicated larger variation in the extraction method of soluble proteins in low salt (0.2 M NaCl) than high salt (1 M NaCl) condition. Considering that the centers of diversity for common bean are different in seed size, the result of Gst statistics showed that bands with relative mobility of 30, 32, 38 and 40 differentiated two weight groups more than other bands. Furthermore, significant differences were observed between these bands for number of pods per plant and number of seeds per plant.

Involvement of a Novel Peptide in the Heat Shock Response of Australian Wheats

1990 ◽  
Vol 17 (4) ◽  
pp. 441 ◽  
Author(s):  
CS Blumenthal ◽  
IL Batey ◽  
CW Wrigley ◽  
EWR Barlow
Keyword(s):  
Heat Shock ◽  
High Performance ◽  
Storage Proteins ◽  
Seed Proteins ◽  
Reversed Phase ◽  
Terminal Sequence ◽  
Chinese Spring Wheat ◽  
End Use ◽  
Peptide Gene

A low molecular weight peptide, induced by exposure of coleoptiles to heat stress at 41°C, has been detected by reversed-phase high performance liquid chromatography of extracts from coleoptiles of five wheat (Triticum aestivum) cultivars. This component is detected within 1 h of a 41°C heat shock, is not detected 48 h after cessation of the heat shock, and remains present during a continuous 24 h heat treatment. The appearance of this component is also induced by exposure of the coleoptile to 0.1 M sodium arsenite or 10% ethanol. When other species such as barley (Hordeum vulgare), soybean (Glycine max), sorghum (Sorghum bicolor), maize (Zea mays), mungbean (Vigna radiata), or rice (Oryza sativa) were examined for the presence of a component eluting in the same position, it was only detected in maize. The amino acid sequence for the heat-induced peptide from wheat was determined to be: V-L-V-P-V-P-Q-L-Q-P-Q-N-Q-P/Q. The sequence of 12 of these amino acids is the same as the N-terminal sequence of α- and β gliadins (wheat endosperm storage proteins). The production of this heat-induced peptide in aneuploids of Chinese spring wheat indicated that the peptide gene was located on the same chromosome arm as one of the gliadin genes. The presence of this gliadin-like peptide in heat-stressed coleoptiles may be due to the presence of five heat shock elements in the gene sequence of gliadins. The potential heat inducibility of the gliadin gene has important implications for end-use quality of wheat. The results also imply that seed proteins may have a function other than storage of nitrogen.

scholarly journals The use of cotyledon proteins to assess the genetic diversity in sweet holm oak

2009 ◽  
Vol 55 (No. 11) ◽  
pp. 526-531 ◽  
Author(s):  
A. Martín M ◽  
R. Navarro-Cerrillo ◽  
P. Ortega ◽  
B. Alvarez J
Keyword(s):  
Genetic Diversity ◽  
Genetic Variability ◽  
Quercus Ilex ◽  
Storage Proteins ◽  
Allelic Variation ◽  
Seed Proteins ◽  
Wide Distribution ◽  
Holm Oak ◽  
Additional Tool ◽  
The Mediterranean Basin

Sweet holm oak (<I>Quercus ilex</I> ssp. <I>ballota</I> Desf. Samp.) is an important broad-leaved tree spread in the Mediterranean basin. In Spain, few studies on the genetic variability of this species have been displayed. Storage seed proteins are a useful tool in the evaluation of the genetic variability of many species. The objective of this study was to analyze the usefulness of cotyledon proteins as markers of the genetic diversity in sweet holm oak. The evaluated populations were highly polymorphic for the glutelins, being detected up to 32 polymorphic bands with a wide distribution among all them. Considering all evaluated populations, about 35.8% of the total allelic variation was distributed among populations. This method of analysis of cotyledon storage proteins (glutelins) could be considered an additional tool for the evaluation of genetic diversity in this species.

Characterization of storage proteins extracted from Avena sativa seed protein bodies

1982 ◽  
Vol 30 (1) ◽  
pp. 32-36 ◽  
Author(s):  
Jean Claude Pernollet ◽  
Su Il Kim ◽  
Jacques Mosse
Keyword(s):  
Avena Sativa ◽  
Seed Protein ◽  
Storage Proteins ◽  
Protein Bodies

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.

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

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.

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