The high-molecular-weight glutenin subunit composition of Japanese hexaploid wheat landraces

2000 ◽  
Vol 51 (6) ◽  
pp. 673 ◽  
Author(s):  
H. Nakamura
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Hexaploid Wheat ◽  
Storage Proteins ◽  
Allelic Variation ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Glutenin Subunit ◽  
Subunit Composition ◽  
Wheat Landraces

The endosperm storage proteins of 174 Japanese wheat (Triticum aestivum) landraces were fractionated by sodium dodecyl sulfate polyacrylamide gel electrophoresis to determine their high-molecular-weight (HMW) glutenin subunit composition. These are alleles for complex gene loci, Glu-A1, Glu-B1, and Glu-D1, that are present in Japanese hexaploid wheat landraces. These were identified by comparison with the subunit mobility previously found in hexaploid wheat. Twenty-four different, major glutenin HMW subunits were identified. Each landrace contained 3–5 subunits, and 17 different glutenin subunit patterns were observed for 13 alleles in Japanese landraces. Japanese landraces showed specific allelic variation in glutenin HMW subunits, different from those in non-Japanese hexaploid wheats.

The association between high molecular weight glutenin subunit compositions and the bread-making quality of Chinese and Japanese hexaploid wheats

2000 ◽  
Vol 51 (3) ◽  
pp. 371 ◽  
Author(s):  
H. Nakamura
Keyword(s):  
Molecular Weight ◽  
Genetic Variation ◽  
High Molecular Weight ◽  
Hexaploid Wheat ◽  
Allelic Variation ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Glutenin Subunit ◽  
Wheat Varieties ◽  
Hmw Glutenin

Variation in the electrophoretic banding patterns of high molecular weight (HMW) glutenin subunits of 274 hexaploid wheat (Triticum aestivum) varieties from China was examined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Twenty-seven different major glutenin HMW subunits were identified. Each variety contained 3–5 subunits and 29 different glutenin subunit patterns were segregated. Seventeen alleles were identified based on comparison of subunit mobilities with those previously found for hexaploid wheat. Chinese hexaploid wheats exhibited particular allelic variation in glutenin HMW subunit composition and this variation differed from that found in wheats from Japanese and other countries. Average Glu-1 quality scores of 274 Chinese wheat varieties in the present study have been shown to be higher than that of Japanese wheats. Considerable genetic variation in the HMW glutenin subunit compositions of the Chinese wheats was observed in the present study and previously. Alleles from Chinese hexaploid wheat varieties have not been extensively introduced into Japan and other countries. The present data may indicate possible applications of Chinese germplasm in wheat breeding programs. To improve the wheat quality, genetic variation should be attempted through the introduction of genes of Chinese varieties into varieties in Japan and other countries.

The high-molecular-weight glutenin subunit composition of Australian wheat cultivars

1986 ◽  
Vol 37 (2) ◽  
pp. 125 ◽  
Author(s):  
GJ Lawrence
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Storage Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Glutenin Subunit ◽  
Subunit Composition ◽  
Wheat Cultivars ◽  
Australian Wheat ◽  
Hmw Glutenin

The seed storage proteins of 106 Australian wheat cultivars were fractionated by sodium dodecyl sulfate polyacrylamide gel electrophoresis to determine the allelic composition of the cultivars at each of the three loci controlling high-molecular-weight (HMW) glutenin subunits. Amongst the cultivars, three alleles were identified at the Glu-A1 locus, eight at the Glu-B1locus and four at the Glu-D1 locus. The results are presented in the form of a key to aid identification of unknown samples. Sixteen of the cultivars were found to consist of two or more biotypes with respect to HMW glutenin subunit composition.

Genetic Diversity of High-Molecular-Weight Glutenin Subunit Composition in Chinese Wheat Landraces

2013 ◽  
Vol 38 (7) ◽  
pp. 1205-1211
Author(s):  
Xin XU ◽  
Xiao-Jun LI ◽  
Ling-Li ZHANG ◽  
Xiu-Quan LI ◽  
Xin-Ming YANG ◽  
...  
Keyword(s):  
Genetic Diversity ◽  
Molecular Weight ◽  
High Molecular Weight ◽  
Glutenin Subunit ◽  
Subunit Composition ◽  
Wheat Landraces ◽  
Chinese Wheat

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 Genetic Diversity of High and Low Molecular Weight Glutenin Subunits in Algerian Aegilops geniculata

2014 ◽  
Vol 42 (2) ◽  
pp. 453-459 ◽  
Author(s):  
Asma MEDOURI ◽  
Inès BELLIL ◽  
Douadi KHELIFI
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Storage Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Low Molecular Weight ◽  
Glutenin Subunits ◽  
Bread Making ◽  
Aegilops Geniculata ◽  
Wide Range

Aegilops geniculata Roth is an annual grass relative to cultivated wheat and is widely distributed in North Algeria. Endosperm storage proteins of wheat and its relatives, namely glutenins and gliadins, play an important role in dough properties and bread making quality. In the present study, the different alleles encoded at the four glutenin loci (Glu-M1, Glu-U1, Glu-M3 and Glu-U3) were identified from thirty five accessions of the tetraploid wild wheat A. geniculata collected in Algeria using Sodium dodecyl Sulfate - Polyacrylamide Gel Electrophoresis (SDS-PAGE). At Glu-M1 and Glu-U1 loci, encoding high molecular weight glutenin subunits (HMW-GS) or A-subunits, 15 and 12 alleles were observed respectively, including one new subunit. B-Low molecular weight glutenin subunits zone (B-LMW-GS) displayed a far greater variation, as 28 and 25 alleles were identified at loci Glu-M3 and Glu-U3 respectively. Thirty two subunits patterns were revealed at the C subunits- zone and a total of thirty four patterns resulted from the genetic combination of the two zones (B- and C-zone). The wide range of glutenin subunits variation (high molecular weight glutenin subunits and low molecular weight glutenin subunits) in this species has the potential to enhance the genetic variability for improving the quality of wheat./span>

Characterization of 1Sty13, a novel high-molecular-weight glutenin subunit from Elymus sibiricus L.

2021 ◽  
pp. 1-4
Author(s):  
Mei Yan ◽  
Muzi Li ◽  
Zaidong Yang ◽  
Feng Yu ◽  
Xuye Du
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Glutenin Subunit ◽  
Predicted Amino Acid Sequence ◽  
Reading Frame ◽  
Elymus Sibiricus ◽  
Dough Quality ◽  
Key Factor

Abstract High-molecular-weight glutenin subunit (HMW-GS) is a key factor affecting dough-processing quality. 1Sty13 is a novel HMW-GS found in the tetraploid species, Elymus sibiricus L. 1Sty13 has faster electrophoretic mobility than the 1Dy12 subunit on sodium dodecyl sulphate (SDS)-polyacrylamide gel electrophoresis. The gene encoding the 1Sty13 subunit was composed of 1803 nucleotide base pairs with an open reading frame that was 599 amino acids in length. Analysis of the predicted amino acid sequence of 1Sty13 indicated that the N-terminal domain was similar to the y-type subunit, whereas the C-terminal domains were similar to the x-type subunit. Five cysteine residues were found in 1Sty13, which is one less than the published HMW-GS in the St genome. The 1Sty13 protein was purified at a scale sufficient for incorporation into flour for the SDS sedimentation test, which indicated that incorporating 1Sty13 improved dough quality.

scholarly journals The interrelations between high- and low-molecular-weight forms of normal and mutant (Krabbe-disease) galactocerebrosidase

1980 ◽  
Vol 189 (1) ◽  
pp. 9-15 ◽  
Author(s):  
Yoav Ben-Yoseph ◽  
Melinda Hungerford ◽  
Henry L. Nadler
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Active Form ◽  
Sodium Dodecyl ◽  
Krabbe Disease ◽  
Low Molecular Weight ◽  
Molecular Weight Form

Galactocerebrosidase (β-d-galactosyl-N-acylsphingosine galactohydrolase; EC 3.2.1.46) activity of brain and liver preparations from normal individuals and patients with Krabbe disease (globoid-cell leukodystrophy) have been separated by gel filtration into four different molecular-weight forms. The apparent mol.wts. were 760000±34000 and 121000±10000 for the high- and low-molecular-weight forms (peaks I and IV respectively) and 499000±22000 (mean±s.d.) and 256000±12000 for the intermediate forms (peaks II and III respectively). On examination by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, the high- and low-molecular-weight forms revealed a single protein band with a similar mobility corresponding to a mol.wt. of about 125000. Antigenic identity was demonstrated between the various molecular-weight forms of the normal and the mutant galactocerebrosidases by using antisera against either the high- or the low-molecular-weight enzymes. The high-molecular-weight form of galactocerebrosidase was found to possess higher specific activity toward natural substrates when compared with the low-molecular-weight form. It is suggested that the high-molecular-weight enzyme is the active form in vivo and an aggregation process that proceeds from a monomer (mol.wt. approx. 125000) to a dimer (mol.wt. approx. 250000) and from the dimer to either a tetramer (mol.wt. approx. 500000) or a hexamer (mol.wt. approx. 750000) takes place in normal as well as in Krabbe-disease tissues.

scholarly journals Characterization of a Novel High-Molecular-Weight Glutenin Subunit Pair 2.6 + 12 in Common Wheat Landraces in the Xinjiang Uygur Autonomous District of China

2007 ◽  
Vol 57 (3) ◽  
pp. 253-255 ◽  
Author(s):  
Hua Cong ◽  
Kanenori Takata ◽  
Tatsuya M. Ikeda ◽  
Mikiko Yanaka ◽  
Hiroshi Fujimaki ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Common Wheat ◽  
Glutenin Subunit ◽  
Autonomous District ◽  
Wheat Landraces
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