Functionality of the 2S Albumin Seed Storage Proteins from Sunflower (Helianthus annuusL.)

1996 ◽  
Vol 44 (5) ◽  
pp. 1184-1189 ◽  
Author(s):  
Jacques Guéguen ◽  
Yves Popineau ◽  
Irina N. Anisimova ◽  
Roger J. Fido ◽  
Peter R. Shewry ◽  
...  
Keyword(s):  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
2S Albumin

Molecular Cloning of 11S Globulin and 2S Albumin, the Two Major Seed Storage Proteins in Sesame†

1999 ◽  
Vol 47 (12) ◽  
pp. 4932-4938 ◽  
Author(s):  
Sorgan S. K. Tai ◽  
Lawrence S. H. Wu ◽  
Emily C. F. Chen ◽  
Jason T. C. Tzen
Keyword(s):  
Molecular Cloning ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
2S Albumin ◽  
11S Globulin

scholarly journals Stable Accumulation of Modified 2S Albumin Seed Storage Proteins with Higher Methionine Contents in Transgenic Plants

1990 ◽  
Vol 94 (3) ◽  
pp. 970-979 ◽  
Author(s):  
Ann De Clercq ◽  
Martine Vandewiele ◽  
Jozef Van Damme ◽  
Philippe Guerche ◽  
Marc Van Montagu ◽  
...  
Keyword(s):  
Transgenic Plants ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
2S Albumin

Seed storage proteins in cultivars and subspecies of alfalfa (Medicago sativa L.)

2000 ◽  
Vol 10 (4) ◽  
pp. 423-434 ◽  
Author(s):  
Joan E. Krochko ◽  
J. Derek Bewley
Keyword(s):  
Medicago Sativa ◽  
Storage Protein ◽  
Species Complex ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Protein Patterns ◽  
2S Albumin ◽  
Two Dimensional Gel Electrophoresis ◽  
11S Globulin

AbstractSeed storage proteins were analysed in 27 varieties of alfalfa (Medicago sativaL.); these included five subspecies (glomerata, caerulea, falcata, hemicycla, praefalcata), seven of the nine sources of Medicago germplasm introduced into North America and a sample of additional cultivars. The protein patterns were remarkably consistent for all of these taxa. One-dimensional and two-dimensional gel electrophoresis revealed only minor differences in polypeptide composition within each of the three major classes of storage protein (7S globulin, 11S globulin, 2S albumin). The slight variations that were found provided no information on either parentage or evolutionary relationships amongst these particular taxa. Nonetheless, persistent and reproducible heterogeneity of some minor polypeptides of 11S globulin (medicagin) may be useful under other circumstances for cultivar identification in alfalfa. Both subfamilies (I and II) of the 11S globulin were strongly expressed in all of the cultivars and subspecies examined. It was concluded that this structural divergence within the 11S storage protein family predated the evolution of the M. sativa L. species complex. Most of the variability in storage proteins was quantitative. However, even this variability was reduced when data were standardized with respect to seed dry weights. The consistent similarities in qualitative and quantitative expression of seed storage proteins amongst all of these taxa suggest a high degree of uniformity in both seed physiology and genetics within the alfalfa species complex.

Gene Families Encoding Isoforms of Two Major Sesame Seed Storage Proteins, 11S Globulin and 2S Albumin†

2006 ◽  
Vol 54 (25) ◽  
pp. 9544-9550 ◽  
Author(s):  
Eric S. L. Hsiao ◽  
Li-Jen Lin ◽  
Feng-Yin Li ◽  
Miki M. C. Wang ◽  
Ming-Yuan Liao ◽  
...  
Keyword(s):  
Storage Proteins ◽  
Sesame Seed ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Gene Families ◽  
2S Albumin ◽  
11S Globulin

scholarly journals Seed Storage Proteins, 2S Albumin And 11S Globulin, Associated to Severe Allergic Reactions after Flaxseed Intake

2021 ◽  
Vol 32 (5) ◽  
Author(s):  
C Bueno-Díaz ◽  
C Biserni ◽  
L Martín-Pedraza ◽  
M de las Heras ◽  
C Blanco ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Storage Proteins ◽  
Binding Capacity ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Cross Reactivity ◽  
2S Albumin ◽  
11S Globulin ◽  
Flaxseed Extract

Background: Given the increased popularity of flaxseed in meals, several cases of allergy to these seeds have been reported. Little is known about allergens implicated in hypersensitivity reactions to these seeds. The present work aimed to identify the allergens involved in IgE-mediated reactions in five patients with a clinical history of severe systemic symptoms after flaxseed consumption. Methods: Proteins susceptible to be allergens with IgE-binding capacity were purified from flaxseed extract by chromatographic techniques. Their identification was achieved via MALDI-TOF mass spectrometry. Immunoassays were performed using the five allergic patient’s era either by testing them individually or as a pool. Results: Four out of five patients recognized a low-molecular-mass protein (around 13kDa) by immunoblotting of the flaxseed extract, while two patients recognized a protein of approximately 55 kDa. They were identified by mass spectrometry as flaxseed 2S albumin, included into WHO/IUIS allergen nomenclature as Lin u 1,and 11S globulin, respectively. Inhibition assays revealed in vitro IgE-cross-reactivity of Lin u 1 with peanut and cashew nut proteins, while IgE recognition of 11S globulin by patients’ sera was partially inhibited by several plant-derived sources. Conclusions: Seed storage proteins from flaxseed were involved in the development of severe symptoms in five individuals and exhibited cross-reactivity with other allergenic sources. Besides the severity of flaxseed allergy in patients sensitized to 2S albumin, it is the first time that the 11S globulin is identified as a potential allergen. We consider that these data should be taken into account for a more accurate diagnosis of patients.

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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