Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    ISSN: 1432-2242
    Keywords: HMW storage prolamins ; Wheat ; Rye ; Barley ; Characterization and purification
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Homologous high molecular weight storage prolamins were purified from grain of wheat, rye and barley using combinations of gel filtration, ion-exchange chromatography and preparative isoelectric focusing. Sodium dodecylsulphate polyacrylamide gel electrophoresis showed that the components were single bands with apparent mol.wts. of above 100,000. Molecular weights determined by sedimentation equilibrium ultracentrifugation were considerably lower; 54,700, 67,600 and 69,600 for the components from barley, rye and wheat respectively. Amino acid analysis showed the presence of 13.6 to 16.5 mol% glycine, 29.6 to 34.0 mol% glutamate + glutamine, 11.4 to 13.7 mol% proline and a total of 4.0 to 5.7 mol% basic amino acids. Automated N-terminal amino acid sequencing of the component from wheat showed the presence of cysteine residues at positions 5 and 10, and this is discussed in relation to the possible role of these proteins in the visco-elastic gluten network.
    Type of Medium: Electronic Resource
    Signatur Availability
    BibTip Others were also interested in ...
  • 2
    ISSN: 1432-2242
    Keywords: RFLP ; Wheat ; Aegilops ; Rye ; β-Amylase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A β-amylase cDNA clone isolated from barley has been used to locate β-amylase encoding sequences on wheat, rye, and Aegilops umbellulata chromosomes by hybridisation to restriction endonuclease digested DNA obtained from wheat aneuploid and wheat-alien addition lines. Structural genes were identified on homoeologous group 4 and 5 chromosomes, confirming the results of isozyme studies. In addition, a further set of structural genes was found on homoeologous group 2 chromosomes. It is proposed that there are two homoeoallelic series, β-Amy-1 on group 4 or 5 chromosomes, and β-Amy-2 on group 2 chromosomes. Evidence is presented that each locus contains one or two β-amylase structural genes, and it is suggested that the large number of isozymes seen upon IEF are due to post-translational modifications.
    Type of Medium: Electronic Resource
    Signatur Availability
    BibTip Others were also interested in ...
  • 3
    ISSN: 1432-2242
    Keywords: Wheat ; Gli-1 loci ; Gliadins ; LMW glutenins ; RFLP
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Probes related to γ-gliadins and to the LMW subunits of glutenin were used to determine the complexity of the Gli-1 loci, by RFLP analysis of euploid and aneuploid lines of bread wheat cv Chinese Spring and durum wheat cv Langdon. The two probes hybridised to separate sets of fragments derived from chromosomes 1 A, 1 B and 1D. The fragments related to the LMW subunit probe had a total copy number in HindIII digests of about 35 in Chinese Spring and 17 in Langdon, with more fragments derived from chromosomes 1D. The fragments hybridising to the γ-gliadin probe could be divided into two classes, based on whether they hybridised to the whole probe at high stringency or to the 3′ nonrepetitive region at moderate stringency. The fragments that failed to hybridise under these conditions were considered to be related to ω-gliadins. The fragments related to γ — and co-gliadins had total copy numbers of about 39 and 16, respectively, in HindIII digests of Chinese Spring, and about 24 and 12, respectively, in Langdon.
    Type of Medium: Electronic Resource
    Signatur Availability
    BibTip Others were also interested in ...
  • 4
    ISSN: 1432-2242
    Keywords: Wheat ; HMW glutenin subunits ; Bread-making quality ; Gene ; Protein sequence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A gene encoding the high-molecular-weight (HMW) subunit of glutenin 1Ax1 was isolated from bread wheat cv Hope. Comparison of the deduced amino acid sequence with that previously reported for an allelic subunit, 1Ax2*, showed only minor differences, which were consistent with both subunits being associated with good bread-making quality. Quantitative analyses of total protein extracts from 22 cultivars of bread wheat showed that the presence of either subunit 1Ax1 or 1Ax2*, when compared with a null allele, resulted in an increase in the proportion of HMW subunit protein from ca. 8 to 10% of the total. It is suggested that this quantitative increase in HMW subunit protein may account for the association of 1Ax subunits with good quality.
    Type of Medium: Electronic Resource
    Signatur Availability
    BibTip Others were also interested in ...
  • 5
    ISSN: 1432-2242
    Keywords: Gliadins ; Glutenins ; Gene location ; Dasypyrum villosum ; Wheat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Genes coding for glutenin-like subunits and for several prolamin subunits with electrophoretic mobilities (lactate-PAGE) corresponding to those of omega- and gamma-gliadins of wheat were located inDasypyrum villosum chromosome1V. Genes controlling four gliadinlike subunits with electrophoretic mobilities corresponding to those of alpha- and gamma-gliadins were located on the short arm of chromosome6V and on the long arm of chromosome4V. N-terminal amino acid sequences of these four components were also determined and homology with alpha-type gliadins was demonstrated. The presence of genes coding for glutenin- and gliadin-like subunits on chromosomes1V and6V demonstrates homoeology between theD. villosum chromosomes1V and6V and the chromosomes of homoeologous groups 1 and 6 in wheat. It is likely that the additional locusGli-V3 on chromosome4V originated by translocation from theGli-V2 locus.
    Type of Medium: Electronic Resource
    Signatur Availability
    BibTip Others were also interested in ...
  • 6
    ISSN: 1432-2242
    Keywords: ‘Null’ forms ; RFLP ; Gliadins ; LMW glutenins ; Deletion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Wheat accessions lacking some of the ω- and γ-gliadin components encoded by the Gli-1 loci on the short arm of chromosome 1D in bread wheat and chromosome 1A in durum wheat were studied by two-dimensional polyacrylamide gel electrophoresis and restriction fragment analysis. Digested genomic DNAs of ‘normal’ and ‘null’ forms were probed with a cDNA clone related to ω-/γ-gliadins and with a genomic clone encoding an LMW subunit of glutenin. The hybridisation patterns with the ω-/γ-gliadin probe were similar to those of cvs ‘Chinese Spring’ and ‘Langdon’ used as standards for bread and durum wheats, respectively, but several restriction fragments located on the 1D chromosome of bread wheat and the 1A chromosome of durum wheat were absent in the ‘null’ forms. In addition, specific LMW glutenin fragments encoded by the same chromosomes were also absent in the ‘null’ forms, suggesting that simultaneous deletions of blocks of genes for both ω-/γ-gliadins and LMW glutenins had occurred. Comparisons of the protein and RFLP patterns enabled some proteins to be mapped to specific restriction fragments.
    Type of Medium: Electronic Resource
    Signatur Availability
    BibTip Others were also interested in ...
  • 7
    ISSN: 1432-2242
    Keywords: Key words Tritordeum ; Transformation ; HMW glutenin subunits ; Seed protein engineering ; Dough functionality
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  The high-molecular-weight (HMW) subunits of wheat glutenin are the major determinants of the gluten visco-elasticity that allows wheat doughs to be used to make bread, pasta and other food products. In order to increase the proportions of the HMW subunits, and hence improve breadmaking performance, particle bombardment was used to transform tritordeum, a fertile amphiploid between wild barley and pasta wheat, with genes encoding two HMW glutenin subunits (1Ax1 and 1Dx5). Of the 13 independent transgenic lines recovered (a transformation frequency of 1.4%) six express the novel HMW subunits at levels similar to, or higher than, those of the endogenous subunits encoded on chromosome 1B. Small-scale mixograph analysis of T2 seeds from a line expressing the transgene for 1Dx5 indicated that the addition of novel HMW subunits can result in significant improvements in dough strength and stability, thus demonstrating that transformation can be used to modify the functional properties of tritordeum for improved breadmaking.
    Type of Medium: Electronic Resource
    Signatur Availability
    BibTip Others were also interested in ...
  • 8
    ISSN: 1432-2242
    Keywords: Rye secalins ; Structural genes ; Secale sp.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Rye secalins are a polymorphic mixture of polypeptides which are classified into four major groups. Previous studies have shown that the structural genes for two of the groups (the ω-secalins and 40K γ-secalins) are located on the short arm of chromosome 1R and those for a third group (the high molecular weight secalins) on the long arm of the same chromosome. Analysis of F2 grain from crosses between inbred lines of S. cereale shows that the structural genes for the ω-secalins (designated Sec 1) and the high molecular weight secalins (designated Sec 3) are loosely linked (40.8 ±3.76% recombination, 57.4 ± 11.30 cM). Analysis of wheat rye addition lines shows that the structural genes for the 75K γ-secalins are present on chromosome 2R. This locus is provisionally designated Sec 2. These genes are probably derived from those for the 40K γ-secalins by duplication, divergence and translocation. Analysis of secalin fractions from wild species of rye shows that all contain 75K γ-secalins, indicating that the duplication and divergence, if not the translocation, occurred before speciation of the genus.
    Type of Medium: Electronic Resource
    Signatur Availability
    BibTip Others were also interested in ...
  • 9
    ISSN: 1432-2242
    Keywords: Glutenin ; Wheat ; Amino acid sequences ; Chromosomes 1A, 1B and 1D
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The nucleotide and deduced amino acid sequences of a high molecular weight glutenin subunit gene derived from chromosome 1B of bread wheat (Triticum aestivum L.) are reported. The encoded protein corresponds to the y-type subunit 1B9. Comparison of the 5′ upstream untranslated regions of this gene and a previously reported silent y-type gene derived from chromosome 1A showed a deletion of 85 bp in the latter. A sequence present in this region of the 1By 9 gene shows homology with part of the “-300 element” which is conserved in the 5′ upstream regions of other prolamin genes from barley, wheat and maize (Forde BG et al. 1985). It is suggested that the absence of this element is responsible for the lack of expression of the 1Ay gene. Comparison of the derived amino acid sequence with those reported previously for the silent 1Ay gene and the expressed x-type (1Dx2) and y-type (1Dy12) genes derived from chromosome 1D showed that the three y-type proteins are closely related. In contrast the x-type subunit (1Dx2) shows clear differences in the N-terminal region and in the number, type and organisation of repeats in the central repetitive domain.
    Type of Medium: Electronic Resource
    Signatur Availability
    BibTip Others were also interested in ...
  • 10
    ISSN: 1432-2242
    Keywords: LMW glutenin subunits ; Monoclonal antibodies ; Baking quality
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A murine monoclonal antibody (IFRN 0067), one of a library developed against prolamin fractions fromTriticum aestivum, has been characterised using a combination of immunoassay and immunoblotting techniques. The antibody was specific for two glutenin polypeptides which appeared by 2-dimensional electrophoresis to belong to the B group of LMW subunits. From results of antibody-binding studies with material extracted from genetic stocks, it was deduced that the target polypeptides were encoded on the short arm of chromosome 1D. The antibody was used in an immunoassay of bread wheats with a range of anticipated baking scores and for flours of known baking performance. Significant correlations were found between immunoassay and test-bake results. Indeed, correlation of IFRN 0067 binding with loaf volume was equal or better than that provided by alveograph parameters. The results provide evidence that LMW subunits contribute to the bread-making properties of wheat glutenin, as identified by the use of immunological techniques. The use of particular monoclonal antibodies, such as IFRN 0067, in the further development of simple, rapid diagnostic tests for flour quality predictions is discussed.
    Type of Medium: Electronic Resource
    Signatur Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...