Differentiate of Ten Pea Cultivars ( Pisum Sativum L. ) by RAPD Markers and Seed Storage Proteins = التفريق بين عشرة أصناف من البازيلاء ( Pisum Sativum L. ) بواسطة تقنية RAPD و بروتينات البذور الخاصة بالتخزين

2015 ◽  
Vol 11 (1) ◽  
pp. 95-107
Author(s):  
Nawroz Abdul-Razzak Tahir ◽  
Hero Fatih Hama Kareem ◽  
Bestwn Omar Hama Amin
Keyword(s):  
Pisum Sativum ◽  
Rapd Markers ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Pisum Sativum L

scholarly journals Convicilin mRNA from pea (Pisum sativum L.) has sequence homology with other legume 7S storage protein mRNA species

1984 ◽  
Vol 224 (2) ◽  
pp. 661-666 ◽  
Author(s):  
R Casey ◽  
C Domoney ◽  
J Stanley
Keyword(s):  
Nucleotide Sequence ◽  
Pisum Sativum ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Nucleotide Sequence Analysis ◽  
Sequence Difference ◽  
Legume Seed ◽  
Complementary Dna ◽  
Pisum Sativum L

Nucleotide-sequence analysis of a complementary-DNA clone for convicilin, one of the storage proteins from pea (Pisum sativum L.) seeds, shows it to be homologous with the 7S legume seed storage proteins vicilin, conglycinin and phaseolin. Convicilin is more similar to vicilin than to phaseolin or to conglycinin. Significant areas of sequence difference are discussed.

Electrophoretic and immunochemical techniques for the molecular reassessment of relationships within Vicieae

2007 ◽  
Vol 55 (2) ◽  
pp. 131-147
Author(s):  
R. Sammour
Keyword(s):  
Pisum Sativum ◽  
Vicia Faba ◽  
Cicer Arietinum ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Immunochemical Study ◽  
Partial Identity ◽  
Electrophoretic Patterns ◽  
Immunochemical Techniques

In this study, an array of electrophoretic and immunochemical techniques was used to investigate the legumins, vicilins and albumins of seed storage proteins in Pisum sativum , Vicia faba , Lens esculentum , and Cicer arietinum to delimit the boundary of the tribe Vicieae and to clarify the systematic position of the genus Cicer . The band patterns of the legumins of these species were broadly similar in that they had bands at Mr 60 kDa which disappeared in the presence of 2-mercaptoethanol, giving rise to two sets of new bands, at Mr approximately 40 kDa and 20 kDa, representing acidic or α and basic or β subunits. The band patterns of the vicilins were also quite similar in that they showed bands at Mr approximately 71 kDa (convicilin) and 50 kDa (vicilin), which were not altered by the presence of 2-mercaptoethanol. Serologically, the legumins of Vicia faba and Lens esculentum exhibited total identity with Pisum legumin antiserum under nonreducing conditions, whereas the legumin of Cicer arietinum exhibited only partial identity, which was attributed to the failure of the low molecular subunit pair (Mr 33 kDa) to react with Pisum legumin antiserum. On the other hand, the vicilins of Vicia faba , Lens esculentum and Cicer arietinum had only partial identity with the vicilin of Pisum sativum , which was due to the failure of a number of subunits along the electrophoretic patterns of these species to react with Pisum sativum vicilin antiserum. The electrophoretic patterns of Vicia faba , Lens esculentum and Cicer arietinum were markedly different for the albumins. However, immunochemically they gave a positive reaction with Pisum major albumin antiserum (Mr 25 kDa) and showed a band with a molecular weight slightly higher than the major albumin of Pisum sativum . Extending the immunochemical study to members of the Phaseoleae, Glycineae, Cajaneae and Diocleae revealed that the vicilin and legumin of Cicer were more closely related to the Vicieae than to these tribes. Thus the data presented in this work recommended the classification of Cicer under Vicieae rather than as a separate tribe Cicerideae .

The genetics of legume storage proteins

1984 ◽  
Vol 304 (1120) ◽  
pp. 349-358 ◽  
Keyword(s):  
Phaseolus Vulgaris ◽  
Pisum Sativum ◽  
Storage Protein ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Mendelian Inheritance ◽  
French Bean ◽  
Messenger Rnas ◽  
Polypeptide Structure

The seed storage proteins of Pisum (pea) and Phaseolus vulgaris (French bean) exhibit genetic variation for polypeptide structure; genetical studies indicate that most of the major storage protein genes exhibit simple, codominant Mendelian inheritance. Biochemical analysis of the storage protein polypeptides and their messenger RNAs shows that the allelic alternatives are probably small families of closely linked structural genes. Two of these genes - those for the major legumin gene family and for convicilin, both from Pisum sativum - have been assigned to specific sites on linkage groups. Genes affecting the synthesis of legumin in Pisum sativum and of phaseolin in Phaseolus vulgaris have been identified.

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.

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