The Electrophoretic Contribution to the Solutions of Taxonomical Problems of Some Lathyrus L. Taxa Growing in Turkey

2020 ◽  
Author(s):  
H. Genc ◽  
İ. Emre ◽  
A. Sahin
Keyword(s):  
Seed Storage Protein ◽  
Extraction Procedure ◽  
Seed Proteins ◽  
Seed Storage ◽  
Morphological Data ◽  
Protein Patterns ◽  
Documentation System ◽  
Natural Habitats ◽  
Protein Assay ◽  
Sds Page

Background: The seed proteins are used as molecular markers to clarify the systematic problems. Also, electrophoretic techniques are safe tools to identify the seed proteins. In present study, it was used the SDS-PAGE technique to solve the taxonomical problems of eight taxa of genus Lathyrus belong to three sections Orobus, Lathyrostylis and Pratensis according to the globulin B and glutelin. Methods: The seed materials were collected from natural habitats and 0.5 g seed were homogenized and centrifuged based on extraction procedure. In addition, the amounts of seed storage protein subfractions were determined by using protein assay. The electrophoretic analysis were performed according to the 12% SDS-PAGE. The gel documentation system (Bio-Rad, USA) was used to analyse the electrophoretic data and UPGAMA was used to construct the dendogram to show the relationships among the species under focus. Results: Current study showed that the species of section Pratensis were different from species of sections Orobus and Lathyrostylis. The differences among the studied taxa shown clearly and all studied taxa were choosen from the protein patterns. Furthermore, present study demonstrated that L. nivalis has the highest globulin B and glutelin. Results of the present study generally supported the morphological data.

scholarly journals Suitability of oat-seed storage-protein markers for identification of cultivars in grain and mixed flour samples

2011 ◽  
Vol 49 (No. 11) ◽  
pp. 486-491 ◽  
Author(s):  
V. Dvořáček ◽  
V. Čurn ◽  
J. Moudrý
Keyword(s):  
Protein Fraction ◽  
Seed Storage Protein ◽  
Seed Storage ◽  
Protein Markers ◽  
Protein Patterns ◽  
Identification Procedure ◽  
Naked Oat ◽  
Sds Page ◽  
Oat Cultivars ◽  
Naked Oats

The objective of this study was an improvement on oat identification procedure for laboratory applications, and the comparison of albumin-globulin and avenin protein patterns in five hulled and naked oat cultivars: Abel (CZ) and Izák (CZ) – naked oats, Auron (CZ), Edmund (D) and Expander (D) – hulled oats. The last object of this study was the authenticity verification of standardly prepared meal samples with various proportions of admixture. It was confirmed that avenins, characterised under SDS-PAGE conditions, are reliable implements for the identification of oat cultivars. It was found that oat grain contains, on the basis of Osborne fractionation, another significant protein fraction – glutelins. The question of the protein fraction analysis that was used for the admixture identification stays still open. In sufficiently different cultivars, the certainty of the admixture detection in meal samples may be high. Nevertheless, in other cases (higher cultivar similarity) it will be necessary to use some other, more sensitive techniques.

scholarly journals Characterization of seed storage protein patterns of four Iranian Pistachios using SDS-PAGE

2010 ◽  
Vol 02 (07) ◽  
pp. 737-740 ◽  
Author(s):  
Ali Akbar Ehsanpour ◽  
Behrokh Shojaie ◽  
Fatemeh Rostami
Keyword(s):  
Storage Protein ◽  
Seed Storage Protein ◽  
Seed Storage ◽  
Protein Patterns ◽  
Sds Page

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

Taxonomic significance of seed protein profiles in Acacia, with special reference to Acacia emilioana

2003 ◽  
Vol 16 (1) ◽  
pp. 35 ◽  
Author(s):  
Alicia L. Lamarque ◽  
Renée H. Fortunato
Keyword(s):  
Seed Protein ◽  
Seed Proteins ◽  
High Concentration ◽  
Protein Patterns ◽  
Qualitative And Quantitative ◽  
Sds Page ◽  
Electrophoretic Data ◽  
Main Protein ◽  
Protein Components ◽  
Total Seed

Total seed proteins of 10 Acacia species were examined by SDS–PAGE. The protein patterns showed qualitative and quantitative differences among the taxa analysed. The main protein components of most species examined had MW's in the range of 38.5–49.0 × 103. Subgenus Aculeiferum differed from subg. Acacia in the presence of a high concentration of proteins in the range of 20–24.5 × 103. Hierarchical clustering of the 10 taxa was undertaken, based on Jaccard distances calculated from electrophoretic data. The species grouped in two main clusters, representing the two subgenera of Acacia that occur in America, namely subg. Acacia and subg. Aculeiferum. The taxonomic placement of Acacia emilioana, a species with uncertain sectional affinity within subg. Aculeiferum, is discussed.

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 Mobilization and synthesis of seed storage and LEA proteins during natural priming of Buddleja cordata and Opuntia tomentosa

2018 ◽  
Vol 96 (1) ◽  
pp. 76 ◽  
Author(s):  
Sandra Alvarado-López ◽  
Ximena Gómez-Maqueo ◽  
Diana Soriano ◽  
Alma Orozco-Segovia ◽  
Alicia Gamboa-de Buen
Keyword(s):  
Protein Fraction ◽  
Seed Storage Protein ◽  
Protein Pattern ◽  
Seed Proteins ◽  
Seed Storage ◽  
Wild Plants ◽  
Lea Proteins ◽  
Priming Process ◽  
Buddleja Cordata ◽  
Control Protein

<p><strong>Background</strong><strong>:</strong> In crop plants, the induction of seed storage protein mobilization and synthesis of LEA family proteins has been extensively described.</p><p><strong>Question</strong><strong>:</strong> Natural priming promotes mobilization and synthesis of seed storage and LEA proteins in wild plants?</p><p><strong>Species</strong> <strong>studied</strong><strong>:</strong> <em>Buddleja cordata </em>and<em> Opuntia tomentosa. </em></p><p><strong>Study</strong> <strong>site</strong><strong>:</strong> Reserva Ecológica del Pedregal de San Angel (REPSA).</p><p><strong>Methods</strong><strong>:</strong> Natural priming treatments were applied to <em>B. cordata</em> and <em>O. tomentosa </em>seeds during one and six months respectively. Phosphorylated proteins fractions were obtained by affinity chromatography from control and treated seeds. Differences in protein pattern between control and treated seeds were determined by electrophoresis and the treated seed proteins were identified by LS/LS/MALDITOF. </p><p><strong>Results</strong><strong>:</strong> The phosphorylated fraction of <em>B. cordata</em> treated seeds presented two proteins that were absent in the control protein fraction. These two proteins were identified as two different 11S globulins.  The phosphorylated fraction of <em>O. tomentosa</em> treated seeds also presented two proteins that were absent in the control protein fraction. These two proteins were identified as a 12S globulin and a LEA protein.</p><p><strong>Conclusion</strong><strong>:</strong> Seeds are subjected to changes in soil water content during their permanence in soil; this natural priming process promotes mobilization and synthesis of storage and LEA proteins that are involved in stress resistance. </p>

Sign in / Sign up

Export Citation Format

Share Document