scholarly journals Study on Seed Protein and Protein Profile Pattern of Chickpea (Cice arietinum L.) by SDS-PAGE under Drought Stress and Fertilization

2015 ◽  
Vol 9 (5) ◽  
pp. 87-90 ◽  
Author(s):  
Vahid Ashrafi ◽  
Hoorieh Pourbozorg ◽  
Nasroallah Moradi Kor ◽  
Abasalt Rostami Ajirloo ◽  
Morteza Shamsizadeh ◽  
...  
Keyword(s):  
Drought Stress ◽  
Seed Protein ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Protein Yield ◽  
Severe Drought ◽  
Stress Treatment ◽  
Sds Page ◽  
Effects Of Drought

A field experiment was performed in order to evaluate the effects of drought stress and application of starter nitrogen fertilizer on seed storage proteins and protein pattern in chickpea cultivars. Experiment was performed in split-factorial using randomized complete block design with three replications. The experiment was laid out in a split-factorial design with drought stress in main plots and cultivar with nitrogen fertilizer in subplots with three replications. The experimental treatments consisted of three levels of drought stress [severe drought stress (S2), moderate drought stress (S1) and no drought stress(S0)] and two cultivars of chickpea consist of Azad and Bivanij and 2 N levels. Plants were either not given any N fertilizer (N0), or fertilized by N fertilizer at the rate of 25 kg ha-1 (N25). The results of this study showed that the effects of drought stress on seed storage proteins and protein yield, effect of cultivars on protein yield were significant. With increase of drought stress seed storage proteins was increased and protein yield decreased. Severe drought stress treatment has the highest seed protein and the control treatment has the lowest seed protein. Non stress treatment has the highest protein yield and the severe  drought stress treatment has the lowest protein yield. The SDS- PAGE results revealed that no effects treatments on the protein banding patterns but the related severe drought stress bands were chromatic, because they have highest protein concentration in some protein bands.DOI: http://dx.doi.org/10.3126/ijls.v9i5.12704

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 Isolation and properties of a metalloproteinase from buckwheat (Fagopyrum esculentum) seeds

1990 ◽  
Vol 272 (3) ◽  
pp. 677-682 ◽  
Author(s):  
M A Belozersky ◽  
Y E Dunaevsky ◽  
N E Voskoboynikova
Keyword(s):  
Storage Proteins ◽  
Limited Proteolysis ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Fagopyrum Esculentum ◽  
Gel Chromatography ◽  
Ph Optimum ◽  
Peptide Bonds ◽  
Sds Page ◽  
Homogeneous Preparation

A homogeneous preparation of metalloproteinase, purified 1000-fold, was obtained from buckwheat (Fagopyrum esculentum) seeds. The Mr of the enzyme, determined by SDS/PAGE, was 34,000 (it was 39,000 by gel chromatography). Its pH optimum was 8.0-8.2 with 13 S globulin, from buckwheat seeds, as substrate. Atomic-absorption spectroscopy revealed the presence of one Zn2+ ion per enzyme molecule. The enzyme was completely inhibited by EDTA (1 mM), zincone (1 mM) and 1, 10-phenanthroline (1 mM). The metalloproteinase performed limited proteolysis of the following seed storage proteins: 13 S globulin from buckwheat seeds and 11 S globulin from soybean (Glycine max) seeds. It hydrolysed three peptide bonds formed by the amino groups of Leu15, Tyr16 and Phe25 in the oxidized B-chain of insulin. In its main properties the enzyme is similar to metalloproteinases of animal and bacterial origin.

Revealing genetic diversity in land races and wild accessions of mungbean [Vigna radiata (L.) Wilczek] using SDS-PAGE of seed storage proteins

2015 ◽  
Author(s):  
Ananya Panda ◽  
Swapan K. Tripathy
Keyword(s):  
Storage Proteins ◽  
Seed Storage Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Land Races ◽  
Sds Page ◽  
Wild Accessions ◽  
Total Seed

Total seed storage protein profiles of 74 mungbean land races, three wild accessions and a popular variety ‘Jyoti’ of Odisha were analysed by Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). 32 genotypes could be clearly identified based on genotype-specific seed protein fingerprints while rest of the test genotypes were categorized into eight protein types. Genotypes included in each protein type had 100% homology and some of these could be duplicates. In this pursuit, a few specific polypeptide markers have been detected for identification of the land races/ genotypes. Dendrogram based on electrophoretic data clustered the genotypes into seven groups at 70% phenon level. Paralakhemundi local, Samarjhola local and Phulbani local-D; and three wild accessions (TCR 20, TCR 213 and TCR 243) were comparatively divergent from other genotypes. Besides, Jyoti, Kalahandi local 2A, Sikri local, kodala local A and TCR 20 were identified to be protein rich with high seed yield. TCR 20 being morphologically similar to mungbean, moderately high protein content and high yielding as well as resistant to drought and bruchids; it may serve as a valuable source genotype in recombination breeding

scholarly journals Subunit composition of seed storage proteins in high-protein soybean genotypes

2010 ◽  
Vol 45 (7) ◽  
pp. 721-729 ◽  
Author(s):  
Ksenija Taski-Ajdukovic ◽  
Vuk Djordjevic ◽  
Milos Vidic ◽  
Milka Vujakovic
Keyword(s):  
Protein Content ◽  
Storage Proteins ◽  
Seed Storage Protein ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
High Protein ◽  
Breeding Programs ◽  
Sds Page ◽  
Soybean Genotypes ◽  
Food Applications

The objective of this work was to quantify the accumulation of the major seed storage protein subunits, β-conglycinin and glycinin, and how they influence yield and protein and oil contents in high-protein soybean genotypes. The relative accumulation of subunits was calculated by scanning SDS-PAGE gels using densitometry. The protein content of the tested genotypes was higher than control cultivar in the same maturity group. Several genotypes with improved protein content and with unchanged yield or oil content were developed as a result of new breeding initiatives. This research confirmed that high-protein cultivars accumulate higher amounts of glycinin and β-conglycinin. Genotypes KO5427, KO5428, and KO5429, which accumulated lower quantities of all subunits of glycinin and β-conglycinin, were the only exceptions. Attention should be given to genotypes KO5314 and KO5317, which accumulated significantly higher amounts of both subunits of glycinin, and to genotypes KO5425, KO5319, KO539 and KO536, which accumulated significantly higher amounts of β-conglycinin subunits. These findings suggest that some of the tested genotypes could be beneficial in different breeding programs aimed at the production of agronomically viable plants, yielding high-protein seed with specific composition of storage proteins for specific food applications.

scholarly journals Use of Seed Protein Profiles to Characterize Peanut Cultivars1

1994 ◽  
Vol 21 (2) ◽  
pp. 152-159 ◽  
Author(s):  
C. M. Bianchi-Hall ◽  
R. D. Keys ◽  
H. T. Stalker
Keyword(s):  
Seed Protein ◽  
Cultivar Identification ◽  
Storage Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Genetic Material ◽  
Seed Storage Proteins ◽  
Molecular Techniques ◽  
Protein Profiles ◽  
Sds Page

Abstract In the last 10 to 15 yr, the development of biotechnology and molecular techniques has allowed great advancements toward the identification of cultivars among plant species. In legumes, the success of cultivar identification depends on the species under investigation, the type and variability of genetic material found in cultivars, and the technology used for investigations. In this study, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was used to assess diversity of peanut (Arachis hypogaea L.) seed protein profiles. The objectives of this investigation were a) to assess diversity of protein profiles in peanuts for cultivar identification using SDS-PAGE and b) to determine the extent of variability of seed storage proteins (SSP) among samples of cultivars originating from different locations. The first study included 34 cultivars grown at Lewiston, NC and the second one included nine cultivars grown at six locations. The results of both studies indicated that it is possible to differentiate between subspecies but not to associate a particular profile with only one specific cultivar. Within subspecies, cultivars clustered in more than one group and most cultivars that grouped together were genetically related.

SDS–PAGE of seed proteins in Festuca (Poaceae): taxonomic implications

1991 ◽  
Vol 69 (7) ◽  
pp. 1425-1432 ◽  
Author(s):  
S. G. Aiken ◽  
S. E. Gardiner
Keyword(s):  
Native Species ◽  
Storage Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Seed Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Banding Patterns ◽  
Ungerminated Seed ◽  
Sds Page ◽  
Species Specific

Taxonomically useful descriptors were provided by the banding patterns of seed storage proteins obtained when extracts of bulked, ungerminated seed samples from commercially available North American native species of Festuca were analyzed by sodium dodecylsulphate polyacrylamide gel electrophoresis (SDS–PAGE). The banding patterns for three species of rough fescues (section Breviaristatae Krivot) indicate that although the taxa are closely related, F. campestris Rydb. (2n = 56) does not appear to be an autoploid of either F. altaica Trin. (2n = 28) or F. hallii (Vasey) Piper (2n = 28). A distinct band corresponding to a molecular weight of 57 000 occurred in the seed protein profiles of all native and commercial samples of Festuca L. analyzed. The profile for F. californica Vasey, questionably section Breviaristatae, also has a band at this position, and is very different from that of F. altaica, F. campestris, and F. hallii. Species-specific banding patterns were observed for F. brachyphylla Schultes, F. saximontana Rydb., F. idahoensis Elmer, and F. trachyphylla (Hackel) Krajina (F. ovina L. s.l., F. longifolia Thuill., F. ovina var. duriuscula auct. amer.). The results support the recognition of subgenus Schedonorus (Beauv.) Peter., and sections Breviaristatae Krivot and Festuca. Key words: Poaceae, Festuca, SDS–PAGE seed proteins.

Karyotype and seed protein analyses of Lycium(Solanaceae) in Iran

1999 ◽  
Vol 56 (2) ◽  
pp. 253-264 ◽  
Author(s):  
M. Sheidai ◽  
Z. Narengi ◽  
M. Khatamsaz
Keyword(s):  
Cluster Analysis ◽  
Statistical Methods ◽  
Chromosome Numbers ◽  
Close Relationships ◽  
Seed Protein ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Multivariate Statistical Methods ◽  
Multivariate Statistical

Twelve populations of six Lycium species were analysed for karyotypie characters and seed storage proteins using multivariate statistical methods. All reported chromosome numbers (mostly new) are 2n = 24 (x = 12). Karyotypes were symmetrical and placed in 1A and 2A classes of Stebbins karyotype classification. Cluster analysis of karyological and protein data revealed variations among the populations of L. depressum and L. ruthenicum, and supports close relationships of L. kopetdaghi and L. depressum with L. makranicum, and L. shawii with L. edgeworthii.

Identification of timothy cultivars by SDS-PAGE analysis of seed storage proteins

1992 ◽  
Vol 72 (4) ◽  
pp. 1215-1222 ◽  
Author(s):  
Q. Cai ◽  
M. R. Bullen
Keyword(s):  
Storage Proteins ◽  
Seed Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Phleum Pratense ◽  
Environmental Stability ◽  
Blue Staining ◽  
Coomassie Blue Staining ◽  
Coomassie Blue ◽  
Sds Page

SDS-PAGE analysis of seed proteins was carried out to identify the cultivars in the forage crop, timothy (Phleum pratense L.). Nineteen cultivars of timothy were examined. Among them five were from Europe and fourteen from North America. In total fifty protein bands were detected in mature seed extract by SDS-PAGE followed by Coomassie blue staining. Except for two pairs, all the cultivars were differentiated by SDS-PAGE analysis of seed storage proteins. In the electrophoretic profile, no protein bands were found to be specific either to European or to North American cultivars which is an indication of their genetic similarity. Twelve samples of cultivar Toro harvested from Alberta and Manitoba (Canada), Idaho and Minnesota (USA) were compared and no significant differences were found in their seed protein banding patterns, which suggests environmental stability of timothy seed proteins.Key words: SDS PAGE, timothy cultivar identification, seed storage proteins

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