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

scholarly journals Evaluation of winter wheat collection in terms of HMW- and LMW-glutenin subunits

2010 ◽  
Vol 46 (Special Issue) ◽  
pp. S96-S99 ◽  
Author(s):  
J. Bradová ◽  
L. Štočková
Keyword(s):  
Molecular Weight ◽  
Winter Wheat ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Low Molecular Weight ◽  
Glutenin Subunits ◽  
Bread Making ◽  
Wheat Varieties ◽  
Lmw Glutenin Subunits ◽  
Winter Wheat Varieties

The composition of high molecular weight (HMW-GS) and low molecular weight (LMW-GS) glutenin subunits was examined in a collection of 86 Czech registered winter wheat varieties. These proteins were analyzed by sodium dodecyl sulphate polyacrylamide gel electrophoresis. An inter-varietal polymorphism of the HMW and LMW glutenin subunits was detected. Twenty-one different patterns for HMW were identified, and eighteen for the LMW-glutenins. The different alleles encoded at the six glutenin loci were determined. Three, six, and four alleles were observed, respectively at the <I>Glu-A1, Glu-</I>B1, and <I>Glu-D1 </I>loci (encoding high HMW-GS). Three, eight, and three alleles of LMW-GS were found, respectively, at the <I>Glu-A3, Glu- B3</I>, and <I>Glu-D3 </I>loci. The evaluated varieties were split into four categories of baking quality, and these variety groups were analyzed for the presence of different HMW-GS and LMW-GS alleles. While the alleles <I>Glu-B1c </I>(7+9), and <I>Glu-D1d </I>(5+10) were detected exclusively in bread wheat varieties, the alleles <I>Glu-B1d </I>(6+8), <I>Glu-D1a </I>(2+12), and <I>Glu-A3e/f </I>only occurred in those varieties that are not suitable for bread-making. &nbsp;

Association of high and low molecular weight glutenin subunits with dough strength in durum wheats (Triticum turgidum ssp. turgidum L. conv. durum (Desf.)) in southern Australia

1996 ◽  
Vol 36 (4) ◽  
pp. 451 ◽  
Author(s):  
CY Liu ◽  
AJ Rathjen
Keyword(s):  
Molecular Weight ◽  
Grain Yield ◽  
Durum Wheat ◽  
Bread Wheat ◽  
Low Molecular Weight ◽  
Wheat Cultivars ◽  
Glutenin Subunits ◽  
Dough Strength ◽  
Hmw Glutenin Subunits ◽  
Hmw Glutenin

A large set of durum wheat lines (79 including 8 advanced Australian breeding lines) randomly collected from 11 countries and 11 bread wheat cultivars were grown in replicated trials at 2 field locations to compare yield and gluten quality. Gluten strength, as measured by the sodium dodecyl sulfate (SDS)-sedimentation (SDSS) test, varied considerably among the durum lines and was associated with the presence of specific glutenins. Unlike some previous reports, the present study showed that durum wheat cultivars having the high molecular weight (HMW) glutenin subunits coded by Glu-B1 genes such as 13 + 16 and 7 + 8 were highly correlated with improved dough strength, which was consistent with the effect of HMW glutenin subunits on dough quality in bread wheat. Cultivars having the low molecular weight (LMW) glutenin allele LMW-2 (or gliadin band r-45) generally gave stronger gluten than lines with allele LMW-1, as reported by earlier workers. The LMW pattern LMW-IIt gave the strongest glutenin. The combined better alleles at Glu-B1 (coded bands 13 + 16, 7 + 8 v. 6 + 8, 20) and Glu-3 (patterns LMW- II, LMW-IIt v. LMW-I) showed linear cumulative effects for dough strength. All the durum lines studied had lower SDSS values than the bread wheat controls (45.8 v. 76.2 mL), though durum wheats tended to possess higher grain protein concentrations (14.0 v. 11.9%) and gave lower grain yield than bread wheat. The Australian advanced lines had higher yield and better dough strength than durums from other countries except those from CIMMYT. The Australian lines also had 1-1.5% higher protein concentration and equal or better grain yield than the bread wheat, suggesting that these lines had potential for commercial use.

Variability of Low-Molecular-Weight, Heat-Modifiable Outer Membrane Proteins of Neisseria meningitidis

1980 ◽  
Vol 30 (3) ◽  
pp. 642-648
Author(s):  
J. T. Poolman ◽  
S. De Marie ◽  
H. C. Zanen
Keyword(s):  
Molecular Weight ◽  
Outer Membrane ◽  
High Molecular Weight ◽  
Outer Membrane Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Low Molecular Weight ◽  
Molecular Weights ◽  
Sds Page ◽  
Index Cases

Analysis of major outer membrane protein (MOMP) profiles of various meningococci by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (SDS-PAGE) revealed the presence of 0 to 2 low-molecular-weight, heat-modifiable MOMPs (molecular weight, 25,000 to 32,000) and 1 to 3 high-molecular-weight MOMPs (molecular weight, 32,000 to 46,000). Heat modifiability was investigated by comparing MOMP profiles after heating in SDS solutions at 100°C for 5 min or at 40°C for 1 h. Low-molecular-weight MOMPs shifted to higher apparent molecular weights after being heated at 100°C. Heat modifiability of high-molecular-weight MOMPs varied among strains; whenever modified these proteins shifted to lower apparent molecular weights after complete denaturation. Variability of low-molecular-weight, heat-modifiable MOMPs was demonstrated when MOMP profiles were compared of (i) isolates from index cases and associated cases and carriers among contacts, (ii) different isolates from the same individual, and (iii) isolates from a small epidemic caused by serogroup W-135. In some cases high-molecular-weight MOMPs revealed quantitative differences among related strains. The observed variability and quantitative differences indicate that MOMP serotyping and typing on the basis of SDS-PAGE profiles (PAGE typing) need careful reevaluation.

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.

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>

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.

Characterisation of high- and low-molecular-weight glutenin subunit genes in Chinese winter wheat cultivars and advanced lines using allele-specific markers and SDS-PAGE

2010 ◽  
Vol 61 (1) ◽  
pp. 84 ◽  
Author(s):  
F. P. Yang ◽  
L. H. Wang ◽  
J. W. Wang ◽  
X. Y. He ◽  
X. K. Zhang ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Molecular Markers ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Low Molecular Weight ◽  
Wheat Cultivars ◽  
Specific Pcr ◽  
Sds Page ◽  
Allele Specific ◽  
Chinese Wheat

Wheat end-use product quality is highly influenced by the composition and quantity of high- and low-molecular-weight glutenin subunits (HMW-GS and LMW-GS). In the present study, 224 Chinese wheat cultivars and advanced lines were characterised for the HMW-GS and LMW-GS with allele-specific PCR markers and sodium-dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The results showed that 56 cultivars (25.0%) carried the allele Glu-D1-1d (Dx5), while 80 cultivars (35.7%) with the allele Glu-B1-2a (By8) produced a 527-bp specific band. Fourteen genotypes (6.3%) with the allele Glu-B1e (Bx20) yielded a 701-bp amplicon with the marker Mar and a 753-bp specific PCR fragment with the marker ZSBy9aF1/R3. Glu-B1h (Bx14+By15) was present in only 1 genotype, and 2 cultivars contained the allele Glu-B1f (Bx13+By16) identified with the marker ZSBy9F2/R2. Four genotypes (1.8%) with the allele Glu-B1-1d (Bx6) gave 695-bp and 830-bp bands, and 5 genotypes (2.2%) with the allele Glu-B1i (Bx17+By18) amplified a 659-bp fragment using the marker Bx. One hundred and six cultivars (47.3%) had the allele Glu-B1-2b (By9), amplifying a 663-bp fragment with the marker ZSBy9aF1/R3; 34 genotypes (15.8%) contained the allele Glu-B3d, generating a 662-bp PCR fragment with the marker gluB3d. Fifteen cultivars (7.0%) with the allele Glu-B3b yielded 1570-bp and 750-bp PCR amplicons with the markers gluB3b and gluB3bef, respectively. The allele Glu-B3h was found in 7 cultivars, generating a 1022-bp PCR fragment with the marker gluB3h. The genotypes detected by SDS-PAGE were mostly consistent with those identified by molecular markers, confirming the utility of the molecular markers. The information for the HMW-GS and LMW-GS in Chinese wheat cultivars will be useful in wheat breeding programs.

Composition of and variation in high- and low-molecular weight glutenin subunits, and omega gliadins in Ethiopian tetraploid wheat germplasm

2006 ◽  
Vol 4 (2) ◽  
pp. 134-143 ◽  
Author(s):  
Faris Hailu ◽  
Eva Johansson ◽  
Arnulf Merker ◽  
Getachew Belay ◽  
Harjit-Singh ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Tetraploid Wheat ◽  
Glutenin Subunit ◽  
Low Molecular Weight ◽  
Glutenin Subunits ◽  
Hmw Glutenin Subunits ◽  
Lmw Glutenin Subunits ◽  
Hmw Glutenin ◽  
Omega Gliadins ◽  
High Degree

A collection of 120 Ethiopian tetraploid wheat accessions was analysed for high-molecular weight (HMW) glutenin subunit, low-molecular weight (LMW) glutenin subunit and omega gliadin composition by SDS–PAGE. For the HMW glutenin subunits, a new allelic variant, 2****, was detected which has not been previously described at the Glu-A1 locus. A high proportion of Glu-A1x banding pattern was observed in durum wheat. For the Glu-B1 locus four different banding patterns were detected. Among those HMW glutenin subunits, 7+8 were the most common, while subunits 14+15 and 6+8 were found to be rare. A high degree of variation was evident for the LMW glutenin subunits and D-zone omega gliadins. The association of the composition of the gluten with quality has been discussed. This wide variation can be used in improving the quality of wheat and to widen its genetic base.

scholarly journals Characterization of proteins from the cytoskeleton of Giardia lamblia

1983 ◽  
Vol 59 (1) ◽  
pp. 81-103 ◽  
Author(s):  
R. Crossley ◽  
D.V. Holberton
Keyword(s):  
Molecular Weight ◽  
Sodium Dodecyl Sulphate ◽  
Giardia Lamblia ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Molecular Size ◽  
Molecular Weights

Proteins from the axonemes and disc cytoskeleton of Giardia lamblia have been examined by sodium dodecyl sulphate/polyacrylamide gel electrophoresis. In addition to tubulin and the 30 X 10(3) molecular weight disc protein, at least 18 minor components copurify with the two major proteins in Triton-insoluble structures. The most prominent minor bands have the apparent molecular weights of 110 X 10(3), 95 X 10(3) and 81 X 10(3). Protein of 30 X 10(3) molecular weight accounts for about 20% of organelle protein on gels. In continuous 25 mM-Tris-glycine buffer it migrates mostly as a close-spaced doublet of polypeptides, which are here given the name giardins. Giardia tubulin and giardin have been purified by gel filtration chromatography in the presence of sodium dodecyl sulphate. Well-separated fractions were obtained that could be further characterized. Both proteins are heterogeneous when examined by isoelectric focusing. Five tubulin chains were detected by PAGE Blue 83 dye-binding after focusing in a broad-range ampholyte gel. Giardin is slightly less acidic than tubulin. On gels it splits into four major and four minor chains with isoelectric points in the pI range from 5.8 to 6.2. The amino acid composition of the giardin fraction has been determined, and compared to Giardia tubulin and a rat brain tubulin standard. Giardins are rich in helix-forming residues, particularly leucine. They have a low content of proline and glycine; therefore they may have extensive alpha-helical regions and be rod-shaped. As integral proteins of disc microribbons, giardins in vivo associate closely with tubulin. The properties of giardins indicate that in a number of respects - molecular size, charge, stoichiometry - their structural interaction with tubulin assemblies will be different from other tubulin-accessory protein copolymers studied in vitro.

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.

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