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 Revealing contrasting genetic variation and study of genetic diversity in urdbean (Vigna mungo (L.) Hepper) using SDS-PAGE of seed storage proteins

2016 ◽  
Vol 7 ◽  
Author(s):  
Swapan Kumar Tripathy ◽  
Priyadarshini Mohanty ◽  
Monalisha Jena ◽  
Gokul Bihari Dash ◽  
Kedareswar Pradhan ◽  
...  
Keyword(s):  
Genetic Variation ◽  
Storage Protein ◽  
Storage Proteins ◽  
Seed Storage Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Similarity Index ◽  
Seed Storage ◽  
Protein Profiling ◽  
Sds Page

<p><strong>Total seed storage protein profiles of 20 urdbean genotypes including the popular variety T9 were analysed by Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). 14 genotypes could be clearly identified based on genotype-specific seed protein fingerprints while rest of the test genotypes were categorized into three protein types. Dendrogram based on electrophoretic data clustered the genotypes into seven groups at 78.5% phenon level.  TU 95-1 with TU 12-25-4 revealed lowest similarity index value (0.33) followed by TU 95-1 with PU 30 and KU 96-3(SI=0.35). Clustering pattern revealed distinctly divergent group formed by TPU 95-1 and TPU 4. These may serve as a valuable source genotype in recombination breeding.   </strong></p><p><strong>Key words: </strong>Seed storage protein profiling, SDS-PAGE, Genetic variation, urdbean.<strong></strong></p>

scholarly journals Phytochemical Evaluation of Moth Bean (Vigna aconitifoliaL.) Seeds and Their Divergence

2016 ◽  
Vol 2016 ◽  
pp. 1-6 ◽  
Author(s):  
Neha Gupta ◽  
Nidhi Shrivastava ◽  
Pramod Kumar Singh ◽  
Sameer S. Bhagyawant
Keyword(s):  
Storage Proteins ◽  
Seed Storage Protein ◽  
Radical Scavenging Activity ◽  
Radical Scavenging ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Molecular Weight Range ◽  
Two Dimensional Gel Electrophoresis ◽  
Moth Bean ◽  
Total Seed

In the present study, phytochemical contents of 25 moth bean (Vigna aconitifolia) seed accessions were evaluated. This includes protease inhibitors, phytic acid, radical scavenging activity, and tannins. The studies revealed significant variation in the contents of theses phytochemicals. Presence of photochemical composition was correlated with seed storage proteins like albumin and globulin. Qualitative identification of total seed storage protein abundance across two related moth bean accessions using two-dimensional gel electrophoresis (2D-GE) was performed. Over 20 individual protein fractions were distributed over the gel as a series of spots in two moth bean accessions. Seed proteome accumulated spots of high intensity over a broad range of pI values of 3–10 in a molecular weight range of 11–170 kDa. In both seed accessions maximum protein spots are seen in the pI range of 6–8.

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.

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.

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.

scholarly journals Assessment of phenotypic and storage protein diversity in exotic barley cultivated in District Dir (Pakistan)

2019 ◽  
Vol 10 (4) ◽  
pp. 400-405
Author(s):  
M. Ali ◽  
M. Nisar ◽  
W. Khan ◽  
T. Naz ◽  
S. U. Zaman ◽  
...  
Keyword(s):  
Quantitative Traits ◽  
Storage Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Minimum Variance ◽  
Mean Value ◽  
Variability Index ◽  
Total Seed ◽  
High Level

A total of 198 exotic barley genotypes were collected from the Gene Bank of the Plant Genetic Resource Institute (PGRI), National Agriculture Research Center (NARC), Islamabad, Pakistan, for the assessment of genetic diversity based on morphological and seed storage proteins. Qualitative and quantitative traits were noted as per IPGRI, 1994 descriptor. Among the quantitative parameters, a high level of genetic variability index was noted in seeds per spike at 79.9% of coefficient of variance followed by biomass per plant which shows 37.4% variance, while minimum variance in quantitative traits was noted in days to germination at 5.4% followed by days to maturity at 3.1% with average mean genetic variation in all quantitative traits at 97.6%. Assay of total seed protein in these exotic accessions was analogue through polyacrylamide gel electrophoresis. A high level of variation was noted in loci (bands) B26 (0.98%) followed by B25 (0.89%), B24 (0.78%),B23 (0.69%) and B01 (0.52%). A similarly low level of variation was detected in B03 (0.16%) followed by B06 (0.18%), B13 (0.19%), B12 (0.21%), B11 (0.23%), B05 (0.24%), B07 (0.25%), B21 (0.34%), B20 (0.35%), B17 (0.39%). The results indicate that the mean value of variation in these accessions is 97.6%. Further assessments and exploration were suggested for these genotypes in multi-climatic zones to satisfy farmers’ need, breeders’ interest and malt-industrial requirements.

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.

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.

Genetic Effects on the Proportions of Conglutin γ and a Subunit of Conglutin β in the Storage Proteins of Lupinus angustifolius L. Seeds

1981 ◽  
Vol 8 (3) ◽  
pp. 277 ◽  
Author(s):  
RN Oram ◽  
JM Gillespie ◽  
RJ Blagrove
Keyword(s):  
Storage Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Lupinus Angustifolius ◽  
Β Subunit ◽  
Partial Dominance ◽  
High Level ◽  
Conglutin Γ

The genetic variability in the proportions of conglutin β and γ components of lupin seed storage proteins was explored in F1, F2 and F3 families generated from a cross between two genotypes of Lupinus angustifolius cv. Uniharvest and a white-seeded selection from CPI 47644. The levels of conglutin γ differed by a factor of two in these parents, but varied continuously in the F2 and F3 families, indicating that the parental difference is due to several genes. These parents also differed in the level of a major conglutin β subunit, with a molecular weight of 30 000. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the storage globulins from individual F1, F2 and F3 seeds showed that the high level in cv. Uniharvest is controlled by an incompletely dominant allele, Bsc, at one locus, whereas the low level in CPI 47644 (white-seeded) is due to homozygosity for the recessive allele, bsc. The partial dominance of the Uniharvest gene suggests that the locus has a regulatory or processing function, so it has been designated beta subunit controller. F3 families differed significantly in the level of the conglutin β subunit in Bsc/- seeds, indicating that other loci with smaller effects also influence the proportion of this subunit. The proportion of the β subunit in any seed depends largely on its own genotype, and not on the genotype of the maternal plant. The proportion of conglutin γ in the storage proteins varied inversely with the proportion of the β subunit. The implications of these results for the genetic improvement of the biological value of lupin protein are discussed.

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