scholarly journals Variation in Glutenin Protein Subunits of Wheat

1980 ◽  
Vol 33 (2) ◽  
pp. 221 ◽  
Author(s):  
GJ Lawrence ◽  
KW Shepherd
Keyword(s):  
Molecular Weight ◽  
Cultivar Identification ◽  
Apparent Molecular Weight ◽  
Glutenin Subunits ◽  
Wheat Evolution ◽  
Protein Subunits ◽  
Electrophoresis System ◽  
Glutenin Protein ◽  
Or Genes ◽  
Band Combinations

The high molecular weight glutenin protein subunits (those with apparent molecular weight in the range 80000 to 140000) of 98 wheat cultivars have been examined using a discontinuous gel-electrophoresis system. The number of bands present in each cultivar ranged from three to five and at least 34 different band patterns were observed. Examination of these patterns revealed that some bands, or band combinations, are mutually exclusive and that they can be assigned to three groups. In one group, two pairs of bands occur as alternatives and these bands are controlled by genes on chromosome 1D of wheat. In the second group, three possibilities occur with cultivars possessing either one of two single bands or neither band. These patterns are controlled by a gene or genes on chromosome 1A. In the third group nine patterns occur, four consisting of single bands and five consisting of a pair of bands. Four of these nine patterns have been shown to be controlled by genes on chromosome 1B. The variation detected in the glutenin subunits is useful for cultivar identification, has a bearing on our understanding of wheat evolution, and raises questions concerning the nature of this variation.

Inheritance of novel high-molecular-weight glutenin subunits in the Tunisian bread wheat 'BT-2288'

Genome ◽  
1988 ◽  
Vol 30 (3) ◽  
pp. 442-445
Author(s):  
R. B. Gupta ◽  
K. W. Shepherd
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Gel Electrophoresis ◽  
Cultivar Identification ◽  
Wheat Cultivar ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Glutenin Subunits ◽  
Bread Making

Using sodium dodecyl sulphate-polyacrylamide gel electrophoresis, three new high-molecular-weight glutenin subunit/subunit combinations were detected in a Tunisian wheat cultivar (BT-2288) and these were designated bands 26, 7 + 11, and 5 + 9. Analysis of 112 testcross seeds revealed that the genes controlling them were additional alleles at Glu-A1, Glu-B1, and Glu-D1 loci, respectively. These alleles enhance the genetic variability available for cultivar identification and possibly for improving the bread-making quality of hexaploid wheat.Key words: Triticum aestivum, Glu-1 loci, high-molecular-weight glutenin subunits.

Physico-Chemical Properties of Recombinant Desulphatohirudin

1990 ◽  
Vol 63 (03) ◽  
pp. 499-504 ◽  
Author(s):  
A Electricwala ◽  
L Irons ◽  
R Wait ◽  
R J G Carr ◽  
R J Ling ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Gel Filtration ◽  
Chemical Properties ◽  
Alpha Helix ◽  
Apparent Molecular Weight ◽  
Correlation Spectroscopy ◽  
Nmr Studies ◽  
Recombinant Hirudin ◽  
Physico Chemical ◽  
Recombinant Molecule

SummaryPhysico-chemical properties of recombinant desulphatohirudin expressed in yeast (CIBA GEIGY code No. CGP 39393) were reinvestigated. As previously reported for natural hirudin, the recombinant molecule exhibited abnormal behaviour by gel filtration with an apparent molecular weight greater than that based on the primary structure. However, molecular weight estimation by SDS gel electrophoresis, FAB-mass spectrometry and Photon Correlation Spectroscopy were in agreement with the theoretical molecular weight, with little suggestion of dimer or aggregate formation. Circular dichroism studies of the recombinant molecule show similar spectra at different pH values but are markedly different from that reported by Konno et al. (13) for a natural hirudin-variant. Our CD studies indicate the presence of about 60% beta sheet and the absence of alpha helix in the secondary structure of recombinant hirudin, in agreement with the conformation determined by NMR studies (17)

The Activation of Human Factor IX

1975 ◽  
Vol 33 (03) ◽  
pp. 553-563 ◽  
Author(s):  
B Østerud ◽  
K Laake ◽  
H Prydz
Keyword(s):  
Molecular Weight ◽  
Sodium Dodecyl ◽  
Apparent Molecular Weight ◽  
Factor Ix ◽  
Factor Vii ◽  
Activate Factor ◽  
Human Factor Ix ◽  
Factor Xia ◽  
Tissue Thromboplastin ◽  
Native Factor

SummaryThe activation of factor IX purified from human plasma has been studied. Factor XIa and kallikrein separately activated factor IX to factor IXa. In both cases factor IX a had an apparent molecular weight of about 42–45000 in sodium dodecyl sul-phate-polyacrylamide disc gel electrophoresis compared with a molecular weight of about 70000 for the native factor IX. The activation by XIa required Ca2+-ions whereas Ca2+-ions did not influence the activation by kallikrein. A mixture of tissue thromboplastin and factor VII or RusselPs-viper venom alone did not activate factor IX. Trypsin activated and plasmin inactivated factor IX.

scholarly journals Genetic diversity of high and low molecular weight glutenin subunits in Saharan bread and durum wheats from Algerian oases

2012 ◽  
Vol 48 (No. 1) ◽  
pp. 23-32 ◽  
Author(s):  
I. Bellil ◽  
M. Chekara Bouziani ◽  
D. Khelifi
Keyword(s):  
Genetic Diversity ◽  
Molecular Weight ◽  
Durum Wheat ◽  
Bread Wheat ◽  
Allelic Variation ◽  
Low Molecular Weight ◽  
Glutenin Subunits ◽  
Lmw Glutenin Subunits ◽  
Genotypic Identification ◽  
Diversity Studies

Saharan wheats have been studied particularly from a botanical viewpoint. Genotypic identification, classification and genetic diversity studies to date were essentially based on the morphology of the spike and grain. For this, the allelic variation at the glutenin loci was studied in a set of Saharan bread and durum wheats from Algerian oases where this crop has been traditionally cultivated. The high molecular weight and low molecular weight glutenin subunit composition of 40 Saharan bread and 30 durum wheats was determined by SDS-PAGE. In Saharan bread wheats 32 alleles at the six glutenin loci were detected, which in combination resulted in 36 different patterns including 17 for HMW and 23 for LMW glutenin subunits. For the Saharan durum wheats, 29 different alleles were identified for the five glutenin loci studied. Altogether, 29 glutenin patterns were detected, including 13 for HMW-GS and 20 for LMW-GS. Three new alleles were found in Saharan wheats, two in durum wheat at the Glu-B1 and Glu-B3 loci, and one in bread wheat at the Glu-B1 locus. The mean indices of genetic variation at the six loci in bread wheat and at the five loci in durum wheat were 0.59 and 0.63, respectively, showing that Saharan wheats were more diverse. This information could be useful to select Saharan varieties with improved quality and also as a source of genes to develop new lines when breeding for quality.

Identification of low-molecular weight glutenin subunits of wheat associated with bread-making quality

2004 ◽  
Vol 123 (4) ◽  
pp. 355-360 ◽  
Author(s):  
W. Maruyama-Funatsuki ◽  
K. Takata ◽  
Z. Nishio ◽  
T. Tabiki ◽  
E. Yahata ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Low Molecular Weight ◽  
Glutenin Subunits ◽  
Bread Making

scholarly journals Nuclear matrix of HeLa S3 cells. Polypeptide composition during adenovirus infection and in phases of the cell cycle.

1977 ◽  
Vol 72 (1) ◽  
pp. 194-208 ◽  
Author(s):  
L D Hodge ◽  
P Mancini ◽  
F M Davis ◽  
P Heywood
Keyword(s):  
Cell Cycle ◽  
Molecular Weight ◽  
Nuclear Matrix ◽  
Apparent Molecular Weight ◽  
Molecular Weight Range ◽  
Weight Range ◽  
Molecular Weights ◽  
Liver Nuclei ◽  
Hela S3 ◽  
Biochemical Analyses

A subnuclear fraction has been isolated from HeLa S3 nuclei after treatment with high salt buffer, deoxyribonuclease, and dithiothreitol. This fraction retains the approximate size and shape of nuclei and resembles the nuclear matrix recently isolated from rat liver nuclei. Ultrastructural and biochemical analyses indicate that this structure consists of nonmembranous elements as well as some membranous elements. Its chemical composition is 87% protein, 12% phospholipid, 1% DNA, and 0.1% RNA by weight. The protein constituents are resolved in SDS-polyacrylamide slab gels into 30-35 distinguishable bands in the apparent molecular weight range of 14,000 - 200,000 with major peptides at 14,000 - 18,000 and 45,000 - 75,000. Analysis of newly synthesized polypeptides by cylindrical gel electrophoresis reveals another cluster in the 90,000-130,000 molecular weight range. Infection with adenovirus results in an altered polypeptide profile. Additional polypeptides with apparent molecular weights of 21,000, 23,000, and 92,000 become major components by 22 h after infection. Concomitantly, some peptides in the 45,000-75,000 mol wt range become less prominent. In synchronized cells the relative staining capacity of the six bands in the 45,000-75,000 mol wt range changes during the cell cycle. Synthesis of at least some matrix polypeptides occures in all phases of the cell cycle, although there is decreased synthesis in late S/G2. In the absence of protein synthesis after cell division, at least some polypeptides in the 45,000-75,000 mol wt range survive nuclear dispersal and subsequent reformation during mitosis. The possible significance of this subnuclear structure with regard to structure-function relationships within the nucleus during virus replication and during the life cycle of the cell is discussed.

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