Revealing contrasting genetic variation and study of genetic diversity in urdbean (Vigna mungo (L.) Hepper) using SDS-PAGE of seed storage proteins
Swapan K. TripathyPriyadarshini MohantyMonalisha JenaG. B. DashK. PradhanPramod Kumar NayakSasmita DashDevraj LenkaDayanidhi MishraPavitra Mohan MohapatraDigbijaya SwainNiranjan Senapati
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<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>Keywords:
Dendrogram
Sodium dodecyl sulfate
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Sodium dodecyl sulfate
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Fifteen species belonging to 3 genera (Onobrychis, Hedysarum and Sartoria), collected from different geographical regions of Turkey were studied for the polypeptide patterns of their seed storage proteins. The variability of seed storage proteins was analysed by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). As many as 72 bands were scored and a dendrogram was constructed using UPGMA (unweighted pair group method with arithmetic mean). The dendrogram of the electrophoretic protein profiles of seeds showed 2 main clusters. While the first cluster with further subclusters included Onobrychis species, the second cluster included Sartoria and Hedysarum species present in 2 separate subclusters. The results showed that Sartoria and Hedysarum are closer to each other than they are to Onobrychis. It is also suggested that Sartoria hedysaroides should be included in the genus Hedysarum. Additionally, it is concluded that seed storage protein profiles could be useful markers in studies of genetic diversity, genetic relationships, and classification of adapted cultivars.
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Apolipoproteins B100 and B48 in human and rat plasma were studied by using sodium dodecyl sulfate (SDS) polyacrylamide gradient gel electrophoresis. On SDS gradient gel electrophoresis, human and rat apoprotein B100 co-migrated and had an apparent Mr=258,000±12,000. Human and rat apoprotein B48 had an apparent Mr=189,000±6,000. The molecular weight of human apoprotein B100 determined by sedimentation equilibrium analysis was 270,000±20,000, which was similar to the value determined by SDS gradient gel electrophoresis. However, on SDS polyacrylamide gel electrophoresis at constant concentration, the relative migration value of human apoprotein B100 was not constant when the concentration of polyacrylamide was changed. These results indicate that SDS gradient gel electrophoresis is more suitable for the analysis of apolipoprotein B's than ordinary SDS polyacrylamide gel electrophoresis.
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Aberrant Migration of Lipopolysaccharide in Sodium Dodecyl Sulfate/Poyacrylamide Gel Electrophoresis
Purified lipopolysaccharides of salmoellae strains were separated by sodium dodecyl sulfate/polyacrylamide gel electrophoresis. Pre‐electrophorees of polyacrylamide gels had no apparent effect on one‐dimensional silver‐stained lipopolysaccharide profiles. However, without pre‐electrophoresis, two‐dimensional and three‐dimensional patterns contained numerous bands with varied migration patterns compared to those in the one‐dimension gels. The lipopolysaccharide was altered within the polyacrylamide gel during electrophoresis. Pre‐electrophoresis of gels eliminated aberrant migration patterns.
Sodium dodecyl sulfate
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Ribosomal protein
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Sodium dodecyl sulfate
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SDS-PAGE is a technique to separate proteins from biological samples according to molecular mass. There are highly virulent and invasive pathogens that rapidly invade the host tissue barriers and causes infection in human body. The goal of this study is to gain better understanding of the molecular mechanism of a special bacteria infection into human biological tissues. To analyze the protein quantity in samples, electrophoresis has been performed. Firstly, polyacrylamide gel has been prepared that consists of stacking gel and separation gel.Polyacrylamide gel line up all the protein samples that loaded in the gel and separates the sample proteins according to molecular mass during electrophoresis. To analyze the protein band, polyacrylamide gel has been stained with the silver nitrate solution. While visualizing the gel, the distinct bands with different intensities have been observed.The size of the band reveals the size of protein. From this, the thicker and darker bands have been observed from cell lysates and membrane lysates instead of tissue samples. The sample with darker band represents higher amount of protein, whereas less bands or no bands can be little protein or no full-length proteins but proteolytic fragments. This allow us to find the diversity and size of proteins that are present in the bacterial samples.
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Molecular-weight size marker
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The glutelin seed storage protein from 80 cultivars of rice (Oryza sativa L.) was analysed by SDS-polyacrylamide gel electrophoresis and 2-dimensional polyacrylamide gel electrophoresis. A deletion of one of the glutelin a subunits, α-3, was found in 16 cultivars. All of these cultivars which show this deletion, belong to the Indica type of rice, not the Japonica type. This suggests that there might be a close relationship between the α-3 subunit deletion and the differentiation or distrrbution of rice.
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