scholarly journals Gel Electrophoresis as a Tool to Study Polymorphism and Nutritive Value of the Seed Storage Proteins in the Grain Sorghum

10.5772/38606 ◽  
2012 ◽  
Author(s):  
Lev Elkonin ◽  
Julia Italianskaya ◽  
Irina Fadeev
Keyword(s):  
Gel Electrophoresis ◽  
Nutritive Value ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Grain Sorghum

Diversity of seed storage proteins in common wheat (Triticum aestivum L.)

2011 ◽  
Vol 9 (2) ◽  
pp. 256-259
Author(s):  
Zuzana Šramková ◽  
Edita Gregová ◽  
Svetlana Šliková ◽  
Ernest Šturdík
Keyword(s):  
Triticum Aestivum ◽  
Common Wheat ◽  
Gel Electrophoresis ◽  
Storage Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Triticum Aestivum L ◽  
Polyacrylamide Gel

The objective of our study was to determine the composition of high-molecular weight-glutenin subunits (HMW-GS) in 120 cultivars of common wheat (Triticum aestivum L.). Fourteen alleles and 34 allelic compositions were detected using sodium dodecyl sulphate-polyacrylamide gel electrophoresis. The most frequent HMW-GS alleles at the Glu-A1, Glu-B1 and Glu-D1 loci were null (57.1%), 7+9 (43.3%) and 5+10 (61.9%), respectively. However, low-frequency HMW-GS alleles were also observed, such as 13+16, 20, 21, 7 and 18, encoded by the Glu-B1 locus, and 4+12, encoded by the Glu-D1 locus. The wheat–rye 1BL.1RS translocation was identified in 25 cultivars, using acid polyacrylamide gel electrophoresis. The Glu-score varied greatly, and some lines reached the maximum value of 10.

Profiling the Seed Storage Protein Among Different Genotypes of Trigonella foenum-graecum L. (Fenugreek)

2019 ◽  
Author(s):  
Nisha . ◽  
Priyanka Khati ◽  
P B Rao
Keyword(s):  
Storage Protein ◽  
Gel Electrophoresis ◽  
Storage Proteins ◽  
Seed Storage Protein ◽  
Sodium Dodecyl ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Protein Band ◽  
Trigonella Foenum Graecum ◽  
Trigonella Foenum Graecum L

A qualitative as well as quantitative categorization of seed storage proteins profiles of 23 genotypes of Trigonella foenum- graecum L. were performed by using sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) for exploring the level of genetic discrepancy at seed storage protein level. Total soluble proteins were resolved on 10% resolving gel. A dendrogram was constructed on the basis of weight of seed storage proteins, which divide total genotypes into two groups further classified into different sub groups containing different genotypes in them. The bands obtained from gel electrophoresis can serve as a potent tool in discrimination of different genotypes on the basis of their protein content. Proteins with molecular weight 66, 43 and 35 kDa were found in all the genotypes except Fgk-76, PR, Rmt-303, PEB and Rmt-361, The 43 kDa protein band was found missing in Fgk-67, AFg-2, AM-2, AFg-4, Fgk-73, although the protein with 35 kDa weight was present in all the genotypes but not in Rmt-303 same as 63 kDa which is not present in Fgk-70 and 55 kDa protein band was found missing in Fgk-67, Afg-4 and Rmt-361.

Phylogeny of Prosopis (Leguminosae) as shown by morphological and biochemical evidence

2007 ◽  
Vol 20 (4) ◽  
pp. 332 ◽  
Author(s):  
Alicia D. Burghardt ◽  
Shirley M. Espert
Keyword(s):  
Gel Electrophoresis ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Morphological Characters ◽  
The Other ◽  
Monophyletic Clade ◽  
Biochemical Evidence ◽  
Outgroup Taxon ◽  
Systematic Relationships

Prosopis L. is a rather primitive genus within the Leguminosae–Mimosoideae. This genus has been divided into five sections on the basis especially of the vegetative diversification of the spines. Three of the sections, Algarobia, Monilicarpa and Strombocarpa, are distributed in America. In order to elucidate systematic relationships between the American sections of Prosopis, a morphological and biochemical phylogeny were obtained. Twenty-two morphological characters were scored for 27 species of Prosopis and the outgroup taxon following polyacrilamide gel electrophoresis of seed storage proteins. The results obtained clearly prove that the secction Strombocarpa is a natural taxon. The section Algarobia, on the other hand, seems to comprise an artificial grouping of species. Members of the series Denudantes appear isolated from the remaining species, therefore this taxon should be treated as a new section within Prosopis. The section Algarobia should be circumscribed to series Chilenses, Ruscifoliae and Pallidae, which are always united in a monophyletic clade. Finally, no evidence was found to confirm the existence of the section Monilicarpa.

Application of chromosome-specific monoclonal antibodies in wheat genetics

Genome ◽  
1992 ◽  
Vol 35 (5) ◽  
pp. 831-837 ◽  
Author(s):  
R. E. Knox ◽  
N. K. Howes ◽  
T. Aung
Keyword(s):  
Monoclonal Antibodies ◽  
Gel Electrophoresis ◽  
Storage Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Polyacrylamide Gel ◽  
Root Tip ◽  
Chromosome Marker

A monoclonal antibody (P24B) to a wheat gliadin protein coded by a gene on the short arm of chromosome 1B was used as a chromosome marker. Somatic chromosome number for the 1B chromosome, as predicted by the level of binding of the antibody to extracts from seeds of single cross F2 and testcross F1 populations, was confirmed with sodium dodecyl sulfate – polyacrylamide gel electrophoresis and root-tip analysis. The implications of monoclonal antibodies as tools for cytogenetic analysis are discussed.Key words: polyacrylamide gel electrophoresis, aneuploid, cytogenetics, seed storage proteins.

scholarly journals Wheat (Triticum aestivum L.) TaHMW1D Transcript Variants Are Highly Expressed in Response to Heat Stress and in Grains Located in Distal Part of the Spike

Plants ◽  
2021 ◽  
Vol 10 (4) ◽  
pp. 687
Author(s):  
Chan Seop Ko ◽  
Jin-Baek Kim ◽  
Min Jeong Hong ◽  
Yong Weon Seo
Keyword(s):  
Heat Stress ◽  
High Temperature ◽  
Temperature Stress ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Grain Filling ◽  
High Temperature Stress ◽  
Two Dimensional Gel Electrophoresis ◽  
Transcript Variants

High-temperature stress during the grain filling stage has a deleterious effect on grain yield and end-use quality. Plants undergo various transcriptional events of protein complexity as defensive responses to various stressors. The “Keumgang” wheat cultivar was subjected to high-temperature stress for 6 and 10 days beginning 9 days after anthesis, then two-dimensional gel electrophoresis (2DE) and peptide analyses were performed. Spots showing decreased contents in stressed plants were shown to have strong similarities with a high-molecular glutenin gene, TraesCS1D02G317301 (TaHMW1D). QRT-PCR results confirmed that TaHMW1D was expressed in its full form and in the form of four different transcript variants. These events always occurred between repetitive regions at specific deletion sites (5′-CAA (Glutamine) GG/TG (Glycine) or (Valine)-3′, 5′-GGG (Glycine) CAA (Glutamine) -3′) in an exonic region. Heat stress led to a significant increase in the expression of the transcript variants. This was most evident in the distal parts of the spike. Considering the importance of high-molecular weight glutenin subunits of seed storage proteins, stressed plants might choose shorter polypeptides while retaining glutenin function, thus maintaining the expression of glutenin motifs and conserved sites.

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.

Sign in / Sign up

Export Citation Format

Share Document