scholarly journals Marker-Assisted Selection for Recognizing Wheat Mutant Genotypes Carrying HMW Glutenin Alleles Related to Baking Quality

2014 ◽  
Vol 2014 ◽  
pp. 1-5 ◽  
Author(s):  
Mohammad Javad Zamani ◽  
Mohammad Reza Bihamta ◽  
Behnam Naserian Khiabani ◽  
Zahra Tahernezhad ◽  
Mohammad Taher Hallajian ◽  
...  
Keyword(s):  
Marker Assisted Selection ◽  
Storage Proteins ◽  
Seed Storage Protein ◽  
Allelic Diversity ◽  
Seed Storage ◽  
D Genome ◽  
Baking Quality ◽  
Dough Quality ◽  
Sds Page ◽  
Hmw Glutenin

Allelic diversity of HMW glutenin loci in several studies revealed that allelic combinations affect dough quality. Dx5 + Dy10 subunits are related to good baking quality and Dx2 + Dy12 are related to undesirable baking quality. One of the most regular methods to evaluate the baking quality is SDS-PAGE which is used to improve baking quality labs. Marker-assisted selection is the method which can recognize the alleles related to baking quality and this method is based on polymerase chain reaction. 10 pairs of specific primers related to Dx2, Dx2.1, Dx5, Dy10, and Dy12 subunits were used for recognizing baking quality of some wheat varieties and some mutant genotypes. Only 5 pairs of them could show the specific bands. All subunits were recognized by the primers except Dx2.1. Some of the primers were extracted from previous studies and the others were designed based on D genome subunits of wheat. SDS-PAGE method accomplished having confidence in these marker’s results. To realize the effect of mutation, seed storage proteins were measured. It showed that mutation had effect on the amount of seed storage protein on the mutant seeds (which showed polymorphism).

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.

Investigation of seed storage protein and bread-making quality of triticale

2000 ◽  
Vol 48 (1) ◽  
pp. 41-50 ◽  
Author(s):  
M. Tohver ◽  
R. Täht ◽  
I. Rahnu ◽  
A. Kann
Keyword(s):  
Seed Storage Protein ◽  
Seed Storage ◽  
Subunit Composition ◽  
Whole Grain ◽  
Bread Making ◽  
Winter Triticale ◽  
Sds Page ◽  
Hmw Glutenin ◽  
Whole Grain Flour

The subunit composition of reduced prolamin fractions of winter triticale cultivars of different pedigrees was investigated by means of SDS-PAGE. A comparative analysis of the electrophoregram patterns of triticale cultivars and those of wheat and rye revealed that each cultivar had a unique pattern. Both the glutenin subunits of wheat and the secalin units of rye could be found in triticale cultivars. Whole-grain flour of triticale and wheat was used in baking experiments. The HMW glutenin subunit composition and baking quality of triticale cultivars were in the predicted correlation. Flour from the triticale cultivars could be used in breadmaking by mixing it with up to 30% wheat flour.

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>

Chromosomal location of seed storage protein genes in the genome of Elytrigia elongata

1986 ◽  
Vol 28 (5) ◽  
pp. 818-830 ◽  
Author(s):  
J. Dvořák ◽  
D. D. Kasarda ◽  
M. D. Dietler ◽  
E.-J. L. Lew ◽  
O. D. Anderson ◽  
...  
Keyword(s):  
Chinese Spring ◽  
Storage Proteins ◽  
Seed Storage Protein ◽  
Seed Storage ◽  
Glutenin Subunit ◽  
Gene Location ◽  
Substitution Lines ◽  
Hmw Glutenin Subunit ◽  
Chromosome Arm ◽  
Hmw Glutenin

Additions of complete and telocentric chromosomes of Elytrigia elongata (Host) Nevski in Triticum aestivum L. 'Chinese Spring' were employed to assign the genes coding for seed storage proteins to chromosome arms in the E. elongata genome. Genes coding for prolamins equivalent to wheat gliadins were found on chromosome arms 1ES and 6Ep. Genes on chromosome arm 1ES, which is presumably the p arm, coded for several components with electrophoretic mobilities (lactate–PAGE) corresponding to those of β-, γ-, and ω- gliadins and those on chromosome arm 6Ep coded for two components with mobilities corresponding to those of β-gliadins. Amino acid sequencing of mixtures of prolamins from E. elongata and from E. pontica (Podp.) Holub, a species closely related to E. elongata, indicated that prolamins of these species correspond to α-type (which includes β-gliadins), γ-type, and ω-type gliadins. Restriction fragments of genomic DNAs from substitution lines of chromosome 6E of E. elongata in 'Chinese Spring' were separated electrophoretically in agarose gels and probed with a cloned α-type gliadin gene from 'Yamhill'. This Southern blot showed that chromosome 6E yields DNA fragments identical in size to those characteristic of the α-gliadin gene cluster that is on chromosome 6A of 'Chinese Spring', 'Cheyenne', and 'Yamhill'. These results indicate that structural genes for prolamins of Elytrigia are similar to those of wheat gliadins and are located on the same chromosome arms as those in Triticum species. A high molecular weight (HMW) protein likely to be a HMW glutenin subunit was located on the long arm of chromosome 1E, which presumably is the q arm; this also is in accordance with the location of HMW glutenin subunit genes in Triticum. It is concluded that the appearance of α-type gliadin genes on chromosomes of homoeologous group 6 in T. aestivum occurred prior to divergence of Triticum and Elytrigia but after the divergence of Secale, Hordeum, and the Triticum–Elytrigia lineages, since neither Secale or Hordeum appear to have α-type genes. It is, however, possible that α-type gliadin genes were deleted from the ancestors of Secale and Hordeum after divergence from the Triticum–Elytrigia lineage.Key words: Elytrigia elongata, gene location, prolamins, gliadins, wheat.

Highly Recombinogenic Regions at Seed Storage Protein Loci on Chromosome 1DS of Aegilops tauschii, the D-Genome Donor of Wheat

Genetics ◽  
2000 ◽  
Vol 155 (1) ◽  
pp. 361-367 ◽  
Author(s):  
Wolfgang Spielmeyer ◽  
Odile Moullet ◽  
André Laroche ◽  
Evans S Lagudah
Keyword(s):  
Genetic Distance ◽  
Storage Protein ◽  
Seed Storage Protein ◽  
Aegilops Tauschii ◽  
Bac Library ◽  
Seed Storage ◽  
D Genome ◽  
Rflp Map ◽  
Genome Donor ◽  
The Relationship

Abstract A detailed RFLP map was constructed of the distal end of the short arm of chromosome 1D of Aegilops tauschii, the diploid D-genome donor species of hexaploid wheat. Ae. tauschii was used to overcome some of the limitations commonly associated with molecular studies of wheat such as low levels of DNA polymorphism. Detection of multiple loci by most RFLP probes suggests that gene duplication events have occurred throughout this chromosomal region. Large DNA fragments isolated from a BAC library of Ae. tauschii were used to determine the relationship between physical and genetic distance at seed storage protein loci located at the distal end of chromosome 1DS. Highly recombinogenic regions were identified where the ratio of physical to genetic distance was estimated to be &lt;20 kb/cM. These results are discussed in relation to the genome-wide estimate of the relationship between physical and genetic distance.

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.

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.

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