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

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.

Variability in the 11S globulin fraction of seed storage proteins ofHelianthus (Asteraceae)

1994 ◽  
Vol 193 (1-4) ◽  
pp. 69-79 ◽  
Author(s):  
Jacques Raymond ◽  
Brahim Mimouni ◽  
Jean-Louis Azanza
Keyword(s):  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Globulin Fraction ◽  
11S Globulin

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

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

Molecular cloning and characterization of two soybean protein disulfide isomerases as molecular chaperones for seed storage proteins

FEBS Journal ◽  
2008 ◽  
Vol 275 (10) ◽  
pp. 2644-2658 ◽  
Author(s):  
Shinya Kamauchi ◽  
Hiroyuki Wadahama ◽  
Kensuke Iwasaki ◽  
Yumi Nakamoto ◽  
Keito Nishizawa ◽  
...  
Keyword(s):  
Molecular Cloning ◽  
Molecular Chaperones ◽  
Storage Proteins ◽  
Soybean Protein ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Protein Disulfide Isomerases ◽  
Disulfide Isomerases ◽  
Protein Disulfide

Involvement of the Golgi apparatus in crystalloid protein deposition in Ricinus communis cv. Hale seeds

1990 ◽  
Vol 68 (11) ◽  
pp. 2353-2360 ◽  
Author(s):  
M. J. Brown ◽  
J. S. Greenwood
Keyword(s):  
Storage Protein ◽  
Castor Bean ◽  
Protein Transport ◽  
Storage Proteins ◽  
Ricinus Communis ◽  
Protein Body ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Protein Bodies ◽  
11S Globulin

The developing endosperm of castor bean has been used extensively as a model system for studies of storage-protein synthesis and processing, yet the path of transport of the storage proteins to the protein bodies has not been elucidated. In this study, immunolocalization of the 11S globulin (crystalloid protein) was performed on sections of acrolein–glutaraldehydefixed, resin-embedded, developing castor bean endosperm. Acrolein allowed rapid fixation of the tissue necessary for preserving the ultrastructure of the endomembrane system while maintaining adequate antigenicity of the target protein. Crystalloid protein was localized in the rough endoplasmic reticulum, the known site of synthesis, and in the dense proteinaceous inclusions within the protein bodies. In addition, significant labelling of Golgi complexes and associated vesicles, 65-nm diameter coated vesicles, and larger 220-nm diameter cytoplasmic vesicles was obtained. The findings provide the first direct evidence that the storage parenchyma cells of developing castor bean endosperm possess well-developed, functional Golgi complexes. This is consistent with previous observations of seed storage proteins in other plant species. The study further suggests that two distinct classes of vesicles are involved in the transport of the 11S globulin to the protein bodies. Key words: Golgi, immunolocalization, protein body, Ricinus communis, storage protein, transport (protein).

scholarly journals Identification and Characterization of Storage Proteins in Zygotic and Somatic Embryos of Geranium (Pelargonium ×hortorum)

2000 ◽  
Vol 125 (4) ◽  
pp. 525-529 ◽  
Author(s):  
R.M. Madakadze ◽  
J.E. Krochko ◽  
T. Senaratna
Keyword(s):  
Somatic Embryos ◽  
Storage Proteins ◽  
Zygotic Embryo ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Zygotic Embryos ◽  
Disulphide Bonds ◽  
Embryo Storage Protein ◽  
11S Globulin

Storage proteins in zygotic and somatic embryos of `Scarlet Orbit Improved', zonal geranium (Pelargonium hortorum L.H. Bail.) were identified and characterized using gel electrophoresis. The major seed storage proteins in zygotic embryos were an 11S globulin and two low molecular weight (LMW1-2) proteins. The 11S globulin consisted of four distinct subunits (53-74 ku), with each subunit being composed of an acidic polypeptide (A1-A4; 28-44 ku) linked via disulphide bonds to a basic polypeptide (B1-B4; 20-25 ku) and was named pelargin. The LMW (15.5 and 12,5 ku) albumins were not linked with disulphide bonds. Mature somatic embryos contained 80% of the proteins in zygotic embryos. Although protein profiles were more distinct in mature somatic embryos compared to nonmature, none of the zygotic embryo storage protein was present in the somatic embryos, indicating lack of complete maturity of somatic embryos. This study identified zygotic embryo proteins and demonstrated that maturation of somatic embryos improves protein content and types of proteins.

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