scholarly journals HMW glutenin variation and rye chromatine presence in wheat genome

2003 ◽  
pp. 43-49
Author(s):  
Dragana Obreht ◽  
Ljiljana Vapa ◽  
Mihajla Davidovic
Keyword(s):  
Null Allele ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Wheat Breeding ◽  
Vegetable Crops ◽  
Glutenin Subunits ◽  
Breeding Programs ◽  
Sds Page ◽  
Hmw Glutenin ◽  
Novi Sad

For estimation of wheat end-product quality during wheat breeding programs composition of high-molecular-weight glutenin subunits (HMW GS) and the presence of 1BL/1RS translations serve as markers due to their profound effects on dough elasticity and viscous properties. Ninety-three wheat genotypes from Institute of Field and Vegetable Crops in Novi Sad have been analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) in order to determine their HMW GS composition and 1BL/1RS translocation presence. Eleven alleles were found at the Glu-1 loci. Subunits 1 and 2*and the null allele N were determined at the Glu-A1 locus. Subunitis 7, 7+9, 7+8, 6+8, 20 and 21 were found at the Glu-B1 locus, subunits 2+12 and 5+10 at the Glu-D1 locus. The 1BL/1RS translocation was discovered in 28 cultivars, although three of them were heterogeneous.

scholarly journals Molecular characterization of glutenin alleles at the Glu-Dl locus

2003 ◽  
pp. 35-41
Author(s):  
Ljiljana Vapa ◽  
Dragana Obreht ◽  
Borislav Kobiljski ◽  
Mihajla Davidovic
Keyword(s):  
Wheat Breeding ◽  
Vegetable Crops ◽  
Glutenin Subunits ◽  
Bread Making ◽  
Dough Strength ◽  
Hmw Glutenin Subunits ◽  
Electrophoresis Method ◽  
Hmw Glutenin ◽  
Novi Sad ◽  
Hmw Glutenins

It is well known that the composition of high-molecular-weight (HMW) glutenin subunits impacts the bread making quality. The HMW subunits 1Dx5-1Dyl0 are typically associated with high dough strength and good bread making quality contrary to 1Dx2-lDyl2 subunits. Bread wheat cultivars from Institute of Field and Vegetable Crops in Novi Sad have been screened for the alleles present at Glu-Dl locus using traditional SDS PAG electrophoresis method and a new PCR based approach. The Glu-Dl locus was screened for two main x-type alleles which code for HMW glutenins 2 and 5, and two main y-type alleles which code for HMW glutenin subunits 10 and 12. Among the analyzed cultivars 55.6% expressed the presence of 1Dx5 and 1Dy10 alleles at the Glu-Dl locus. These results confirmed that by using marker-assisted selection (MAS) it is possible to identify genotypes with alleles for good bread making quality which could be successfully used in wheat breeding programs.

IDENTIFICATION OF CANADIAN AND AMERICAN WHEAT CULTIVARS BY SDS GRADIENT PAGE ANALYSIS OF GLIADIN AND GLUTENIN SUBUNITS

1987 ◽  
Vol 67 (4) ◽  
pp. 945-952 ◽  
Author(s):  
B. A. MARCHYLO
Keyword(s):  
Molecular Weight ◽  
Spring Wheat ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Low Molecular Weight ◽  
Wheat Cultivars ◽  
Glutenin Subunits ◽  
Molecular Weights ◽  
Additional Protein ◽  
Hmw Glutenin

Sodium dodecyl sulphate gradient polyacrylamide gel electrophoresis (SDSGPAGE) was used to resolve gliadin and high- and low-molecular-weight glutenin subunits from 19 registered Canadian spring wheat cultivars eligible for Canada Western Red Spring (CWRS) and Canada Prairie Spring (CPS) wheat grades and eight nonregistered spring wheat cultivars from the U.S.A. Reproducible molecular weight estimates were obtained for wheat proteins of apparent molecular weights ranging from 34 238 to 136 174 (avg. CV = 0.72%). Eight different patterns of HMW glutenin subunits consisting of 7–11 protein bands were observed for the 27 cultivars and their biotypes. SDSGPAGE was able to discriminate among the majority of cultivars with all non-registered cultivars and their biotypes distinguishable from registered cultivars. Separation of glutenin subunits along with gliadins provided additional protein bands which assisted in the discrimination of cultivars.Key words: SDS gradient PAGE, wheat cultivar identification, gliadin, glutenin subunits

An approach for isolating high-molecular-weight glutenin subunit genes using monoclonal antibodies

Genome ◽  
2006 ◽  
Vol 49 (2) ◽  
pp. 181-189 ◽  
Author(s):  
H Q Wang ◽  
X Y Zhang
Keyword(s):  
Molecular Weight ◽  
Monoclonal Antibody ◽  
Triticum Aestivum ◽  
Amino Acid ◽  
High Molecular Weight ◽  
Storage Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Glutenin Subunits ◽  
Sds Page

High-molecular-weight glutenin subunits (HMW-GSs) play an important role in the breadmaking quality of wheat flour. In China, cultivars such as Triticum aestivum 'Xiaoyan No. 6' carrying the 1Bx14 and 1By15 glutenin subunits usually have attributes that result in high-quality bread and noodles. HMW-GS 1Bx14 and 1By15 were isolated by preparative sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) and used as an antigen to immunize BALB/c mice. A resulting monoclonal antibody belonging to the IgG1 subclass was shown to bind to all HMW-GSs of Triticum aestivum cultivars, but did not bind to other storage proteins of wheat seeds in a Western blot analysis. After screening a complementary DNA expression library from immature seeds of 'Xiaoyan No. 6' using the monoclonal antibody, the HMW-GS 1By15 gene was isolated and fully sequenced. The deduced amino acid sequence showed an extra stretch of 15 amino acid repeats consisting of a hexapeptide and a nonapeptide in the repetitive domain of this y-type HMW subunit. Bacterial expression of a modified 1By15 gene, in which the coding sequence for the signal peptide was removed and a BamHI site eliminated, gave rise to a protein with mobility identical to that of HMW-GSs extracted from seeds of 'Xiaoyan No. 6' via SDS-PAGE. This approach for isolating genes using specific monoclonal antibody against HMW-GS genes is a good alternative to the extensively used polymerase chain reaction (PCR) technology based on sequence homology of HMW-GSs in wheat and its relatives.Key words: wheat, HMW-GS, monoclonal antibody, immunoscreen.

scholarly journals Conformational differences between two wheat (Triticum aestivum) ‘high-molecular-weight’ glutenin subunits are due to a short region containing six amino acid differences

1989 ◽  
Vol 263 (3) ◽  
pp. 837-842 ◽  
Author(s):  
A P Goldsbrough ◽  
N J Bulleid ◽  
R B Freedman ◽  
R B Flavell
Keyword(s):  
Molecular Weight ◽  
Triticum Aestivum ◽  
Amino Acid ◽  
High Molecular Weight ◽  
Polyacrylamide Gel Electrophoresis ◽  
Amino Acid Sequences ◽  
Glutenin Subunits ◽  
Sds Page ◽  
Hmw Glutenin

‘High-molecular-weight’ (HMW, high-Mr) glutenin subunits are protein constituents of wheat (Triticum aestivum) seeds and are responsible in part for the viscoelasticity of the dough used to make bread. Two subunits, numbered 10 and 12, are the products of allelic genes. Their amino acid sequences have been derived from the nucleic acid sequences of the respective genes. Subunit 10 has fewer amino acids than subunit 12, but migrates more slowly on SDS/PAGE (polyacrylamide-gel electrophoresis). This anomaly is due to between one and six of the amino acid differences between the subunits, localized towards the C-terminal end of the proteins. This has been established by making chimaeric genes between the genes for subunits 10 and 12, transcribing and translating them in vitro and analysing the products by SDS/PAGE. The postulated conformational differences between subunits 10 and 12 are discussed in relation to current hypotheses for the structure of HMW glutenin subunits.

The high molecular weight glutenin subunit composition in old and modern bread wheats cultivated in Iran

2006 ◽  
Vol 57 (10) ◽  
pp. 1109 ◽  
Author(s):  
Ali-Akbar Shahnejat-Bushehri ◽  
Masoud Gomarian ◽  
Bahman Yazdi-Samadi
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecylsulfate ◽  
Quality Parameters ◽  
Wheat Breeding ◽  
Quality Score ◽  
Glutenin Subunit ◽  
Breeding Programs ◽  
Sds Page

All current and old wheat cultivars grown in Iran were characterised by sodium dodecylsulfate polyacrylamide gel electrophoresis (SDS-PAGE). The high-molecular-weight glutenin subunit (HMW-GS) banding patterns for each cultivar were assigned a Glu-1 quality score, a theoretical quality score based on Payne’s Glu-1 quality assignments. At the Glu-A1 loci, HMW-GS subunit compositions N, 7 + 8, 2 + 12 and 2*, 7 + 8, 2 + 12 were found to be predominant being expressed in 24 and 15 cultivars, respectively, out of 95. Eighteen different alleles were identified for the 3 loci studied: Glu-A1 (3), Glu-B1 (9), and Glu-D1 (6). The glutenin quality scores of Iranian wheat ranged from 4 to 10, with an average of 7.4. It was found that some cultivars were heterogeneous in HMW-GS composition. In cv. Cooleh, only one glutenin subunit at the Glu-B1 locus was present. HMW-GS 2*** + 12′ was found in 6 cultivars and biotypes. The results obtained here describing the allelic composition of bread wheat commonly grown in Iran may be useful in wheat breeding programs selecting for good quality parameters.

scholarly journals Glu-B2, a storage protein locus controlling the D group of LMW glutenin subunits in bread wheat (Triticum aestivum)

1985 ◽  
Vol 46 (1) ◽  
pp. 11-17 ◽  
Author(s):  
Elizabeth A. Jackson ◽  
Linda M. Holt ◽  
Peter I. Payne
Keyword(s):  
Molecular Weight ◽  
Storage Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Chromosome 1 ◽  
Glutenin Subunits ◽  
Protein Locus ◽  
Lmw Glutenin Subunits ◽  
Hmw Glutenin ◽  
D Subunit

SUMMARYGenes controlling the synthesis of the D group of low-molecular-weight (LMW) subunits of glutenin occur on the short arms of chromosomes 1B and 1 D. Their position on chromosome 1 B, relative to the storage protein loci Glu-B1 (long arm) and Gli-B1 (short arm), was estimated by analysing the backcross-one progeny of two different crosses. To estimate recombination between the D subunit genes and Gli-B1, half grains were analysed by two-dimensional electrophoresis. The Gli-B1 locus contains genes for the B group of LMW glutenin subunits, γ-gliadins and ω-gliadins although only the latter were made use of in this study to distinguish the parental alleles. Additionally, the complementary half grains were analysed by sodium dodecyl sulphate, polyacrylamide-gel electrophoresis to estimate recombination between Gli-B1 and Glu B1, coding for high-molecular-weight (HMW) glutenin subunits. The D subunit genes occur at a new locus, provisionally defined as Glu-B2, which lies in between Glu-B1 and Gli-B1, 17 cM from the former and 22 cM from the latter. On the basis of previous mapping data involving Gli-B1, it was concluded that the D subunit genes occur close to the nucleolar organizing region and probably on the short-arm satellite, like Gli-B1.

Analysis of high-molecular-weight glutenin subunits in five amphidiploids and their parental diploid species Aegilops umbellulata and Aegilops uniaristata

2014 ◽  
Vol 13 (2) ◽  
pp. 186-189 ◽  
Author(s):  
Shoufen Dai ◽  
Li Zhao ◽  
Xiaofei Xue ◽  
Yanni Jia ◽  
Dengcai Liu ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Triticum Turgidum ◽  
Chromosome Doubling ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Diploid Species ◽  
Glutenin Subunits ◽  
Aegilops Umbellulata ◽  
Sds Page

Amphidiploids serve as a bridge for transferring genes from wild species into wheat. In this study, five amphidiploids with AABBUU and AABBNN genomes were produced by spontaneous chromosome doubling of unreduced triploid F1 gametes from crosses between diploid Aegilops (A. umbellulata accessions CIae 29 and PI 226500, and A. uniaristata accession PI 554419) and tetraploid Triticum turgidum (ssp. durum cultivar Langdon and ssp. dicoccum accessions PI 94 668 and PI 349045) species. The composition of high-molecular-weight glutenin subunits (HMW-GS) in these amphidiploids and in their parental A. umbellulata and A. uniaristata species was analysed. As expected, the amphidiploids from T. turgidum ssp. dicoccum accession PI 944668 or PI 349045 and A. umbellulata accession CIae 29 or PI 226500 and A. uniaristata accession PI 554419 showed the same HMW-GS patterns as those of their Aegilops parents, because HMW-GS genes were all silenced in the T. turgidum ssp. dicoccum parents. The amphidiploids from CIae 29 and Langdon inherited all of the HMW-GS genes from their parents except for the Uy type. Using 10 and 15% sodium dodecyl sulphate–polyacrylamide gel electrophoresis (SDS–PAGE) and 10% urea/SDS–PAGE, 11 Ux and ten Uy types in 16 combinations were observed in 48 A. umbellulata accessions, and two Nx and two Ny types in two combinations were detected in six A. uniaristata accessions. These novel HMW-GS variants may provide new genetic resources for improving the quality of wheat.

scholarly journals Correlation between high molecular weight gluten subunits composition and bread-making quality in Brazilian wheat

1997 ◽  
Vol 20 (4) ◽  
pp. 667-671 ◽  
Author(s):  
Ivan Schuster ◽  
Moacil Alves de Souza ◽  
Antônio Américo Cardoso ◽  
Carlos Sigueyuki Sediyama ◽  
Maurílio Alves Moreira
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Sodium Dodecyl ◽  
Glutenin Subunits ◽  
Bread Making ◽  
Hmw Glutenin Subunits ◽  
Statistical Correlations ◽  
Sds Page ◽  
Half Seed ◽  
Hmw Glutenin

Bread-making quality is one of the most important targets in the genetic improvement of wheat. Although extensive analyses of quality traits such as farinography, sodium dodecyl sulfate (SDS) sedimentation, alveography, and baking are made in breeding programs, these analyses require high amounts of seeds which are obtained only in late generations. In this experiment the statistical correlations between the high molecular weight subunit of glutenin and bread-making quality measured by alveograph, farinograph and SDS sedimentation were evaluated. Seventeen wheat genotypes were grown under the same conditions, each producing about 1 kg of seeds for the evaluations. The high molecular weight (HMW) glutenin subunits were analyzed by SDS-PAGE. Statistical correlations were highly significant between HMW glutenin subunits and alveograph and SDS sedimentation. These results indicate the possibility of manipulating major genes for wheat seed quality by coupling traditional breeding with non-destructive single seed analysis. Only half seed is necessary to perform the SDS-PAGE analysis. Therefore, the other half seed can be planted to generate the progeny. Seed yield and SDS sedimentation were statistically correlated, indicating the possibility of simultaneous selection for both traits

Heterozygous Abnormal Fibrinogen Osaka III with the Replacement of γ Arginine-275 by Histidine Has an Apparently Higher Molecular Weight γ-Chain Variant

1992 ◽  
Vol 68 (05) ◽  
pp. 534-538 ◽  
Author(s):  
Nobuhiko Yoshida ◽  
Shingi Imaoka ◽  
Hajime Hirata ◽  
Michio Matsuda ◽  
Shinji Asakura
Keyword(s):  
Molecular Weight ◽  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Tetraacetic Acid ◽  
Fibrin Monomer ◽  
Sds Page ◽  
Thrombotic Tendency ◽  
Chain Variant

SummaryCongenitally abnormal fibrinogen Osaka III with the replacement of γ Arg-275 by His was found in a 38-year-old female with no bleeding or thrombotic tendency. Release of fibrinopeptide(s) by thrombin or reptilase was normal, but her thrombin or reptilase time in the absence of calcium was markedly prolonged and the polymerization of preformed fibrin monomer which was prepared by the treatment of fibrinogen with thrombin or reptilase was also markedly defective. Propositus' fibrinogen had normal crosslinking abilities of α- and γ-chains. Analysis of fibrinogen chains on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) in the system of Laemmli only revealed the presence of abnormal γ-chain with an apparently higher molecular weight, the presence of which was more clearly detected with SDS-PAGE of fibrin monomer obtained by thrombin treatment. Purified fragment D1 of fibrinogen Osaka III also seemed to contain an apparently higher molecular weight fragment D1 γ remnant on Laemmli gels, which was digested faster than the normal control by plasmin in the presence of [ethy-lenebis(oxyethylenenitrilo)]tetraacetic acid (EGTA).

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