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  • 1
    Electronic Resource
    Electronic Resource
    Fluorescence immunoassay for angiotensin I
    Amsterdam : Elsevier
    Analytica Chimica Acta 170 (1985), S. 133-137 
    Details
    ISSN: 0003-2670
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/S0003-2670(00)81735-3
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  • 2
    Electronic Resource
    Electronic Resource
    A sensitive enzyme immunoassay for angiotensin II in serum
    Amsterdam : Elsevier
    Journal of Pharmaceutical and Biomedical Analysis 12 (1994), S. 1411-1416 
    Details
    ISSN: 0731-7085
    Keywords: Enzyme immunoassay ; angiotensin II.
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology , Medicine
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0731-7085(94)00082-4
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  • 3
    Electronic Resource
    Electronic Resource
    Fluorescence immunoassay for angiotensin I
    Amsterdam : Elsevier
    Analytica Chimica Acta 170 (1985), S. 133-137 
    Details
    ISSN: 0003-2670
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/S0003-2670(00)81735-3
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  • 4
    Electronic Resource
    Electronic Resource
    Reception des ondes decametriques de Jupiter
    Amsterdam : Elsevier
    Icarus 18 (1973), S. 220-221 
    Details
    ISSN: 0019-1035
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0019-1035(73)90205-4
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  • 5
    Electronic Resource
    Electronic Resource
    Science policy in Australia (1988)
    [s.l.] : Nature Publishing Group
    Nature 336 (1988), S. 10-10 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] SIRá€"The Australian federal government has placed great emphasis on science and technology to underpin Australia's future economic performance. A recent policy statement on higher education describes the government's agenda for sweeping changes designed to align academic and ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/336010a0
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  • 6
    Electronic Resource
    Electronic Resource
    The low-molecular-weight glutenin subunit proteins of primitive wheats. II. The genes from A-genome species (1999)
    Springer
    Theoretical and applied genetics 98 (1999), S. 126-134 
    Details
    ISSN: 1432-2242
    Keywords: Key words Low-molecular-weight glutenin subunit proteins ; Gene sequence ; Expression in bacteria ; A genome wheats
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  Three accessions of T. boeoticum were selected for the cloning and sequencing of novel low-molecular-weight glutenin subunit (LMW-GS) genes, based on the results of SDS-PAGE and PCR analyses of the LMW-GS diversity in A-genome wheat (Lee et al. 1998 a). A comparison of the nucleotide and deduced amino-acid sequences of three cloned genes, LMWG-E2, LMWG-E4 and LMWG-AQ1, both to each other and to other known LMW-GS genes was carried out. The N-terminal domains showed one variable position; GAG (coding for a glutamic acid) for the E-type, and GAT (coding for an aspartic acid) for the Q-type. The comparisons of the LMW-GSs in the literature and this paper define three different types of N-terminal sequences; METSCIPGLERPW and MDTSCIPGLERPW from the durum and A-genome wheats, and METRCIPGLERPW from the hexaploid and D-genome wheats. The repetitive domains were AC-rich at the nucleotide level and coded for a large number of glutamine residues; this region showed 16 variable positions changing 12 amino-acid residues, three triple nucleotide deletions/additions, a large deletion of 18 nucleotides in LMWG-E4 and a deletion of 12 nucleotides in LMWG-E2. In the C-terminal domains 26 variable positions were found and 12 of these mutations changed amino-acid residues; no deletions/ additions were present in this region. It was shown that the LMWG-E2 and LMWG-E4 genes could be expressed in bacteria and this allowed the respective protein products to be related back to the proteins defined as LMW-GSs in vivo.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s001220051049
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  • 7
    Electronic Resource
    Electronic Resource
    The low-molecular-weight glutenin subunit proteins of primitive wheats. I. Variation in A-genome species (1999)
    Springer
    Theoretical and applied genetics 98 (1999), S. 119-125 
    Details
    ISSN: 1432-2242
    Keywords: Key words Low-molecular-weight glutenin subunits ; A genome wheats ; Tris-Tricine PAGE ; Variation in genes by PCR
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  A Tris-Tricine gel-electrophoresis system (Schaegger and von Jagow 1987), combined with a gradient gel, has been employed to provide an improved resolution of the B and C low-molecular-weight glutenin subunits (LMW-GSs) found in the endosperm of wheat grain. The gel system was used to document the variation in the gluten subunit proteins present in A-genome diploid wheats. The majority of LMW-GSs found in the A-genome diploid wheats were not present in normal bread wheats; the data suggest that they represent a rich source of new variation for the LMW-GSs which are considered to be very important in modulating wheat flour-processing properties. The analysis of variation in the nature of the LMW-GS genes, using PCR, demonstrated that the subclass of C-subunits assayed by primers from a previously published sequence did not show as much variation as the proteins. However, the data collected suggest that sufficient variation may exist in the LMW-GS genes of A-genome diploid wheats to use them as a source of genes for altering the flour-processing properties of hexaploid wheat.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s001220051048
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  • 8
    Electronic Resource
    Electronic Resource
    The low-molecular-weight glutenin subunit proteins of primitive wheats. IV. Functional properties of products from individual genes (1999)
    Springer
    Theoretical and applied genetics 98 (1999), S. 149-155 
    Details
    ISSN: 1432-2242
    Keywords: Key words Low-weight glutenin subunits ; Single proteins ; extensibility ; Dough properties
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  Three genes encoding the low-molecular-weight glutenin subunits (LMW-GSs), LMWG-E2 and LMWG-E4, from A-genome diploid wheat species, and LMW-16/10 from a D-genome diploid wheat, were expressed in bacteria. The respective proteins were produced on a relatively large scale and compared with respect to their effects on flour-processing properties such as dough mixing, extensibility and maximum resistance; these are important features in the end-use of wheat for producing food products. The LMWG-E2 and LMWG-E4 proteins caused significant increases in peak resistance and mixing time, compared to the control, when incorporated into dough preparations. The LMWG-16/10 protein was qualitatively less effective in producing these changes. All three proteins also conferred varying degrees of decrease in dough breakdown. LMWG-E2 and LMWG-E4 caused significant increases in dough extensibility, and decreases in maximum resistance, relative to the control. LMW-16/10 did not show a significant effect on extensibility but showed a significant decrease in maximum resistance. The refinement of relating specific features of the structure of the LMW-GS genes to the functional properties of their respective proteins is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s001220051051
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  • 9
    Electronic Resource
    Electronic Resource
    Characterisation of a gene encoding wheat endosperm starch branching enzyme-I (1999)
    Springer
    Theoretical and applied genetics 98 (1999), S. 156-163 
    Details
    ISSN: 1432-2242
    Keywords: Key words Triticum tauschii ; Starch branching enzyme genes ; Wheat ; Endosperm
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  A genomic DNA fragment from Triticum tauschii, the donor of the wheat D genome, contains a starch branching enzyme-I (SBE-I) gene spread over 6.5 kb. This gene (designated wSBE I-D4) encodes an amino acid sequence identical to that determined for the N-terminus of SBE-I from the hexaploid wheat (T. aestivum) endosperm. Cognate cDNA sequences for wSBE I-D4 were isolated from hexaploid wheat by hybridisation screening from an endosperm library and also by PCR. A contiguous sequence (D4 cDNA) was assembled from the sequence of five overlapping partial cDNAs which spanned wSBE I-D4. D4 cDNA encodes a mature polypeptide of 87 kDa that shows 90% identity to SBE-I amino acid sequences from rice and maize and contains all the residues considered essential for activity. D4 mRNA has been detected only in the endosperm and is at a maximum concentration mid-way through grain development. The wSBE I-D4 gene consists of 14 exons, similar to the structure for the equivalent gene in rice; the rice gene has a strikingly longer intron 2. The 3′ end of wSBE I-D4 was used to show that the gene is located on group 7 chromosomes. The sequence upstream of wSBE I-D4 was analysed with respect to conserved motifs.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s001220051052
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  • 10
    Electronic Resource
    Electronic Resource
    Cloning and characterization of a gene encoding wheat starch synthase I (1999)
    Springer
    Theoretical and applied genetics 98 (1999), S. 1208-1216 
    Details
    ISSN: 1432-2242
    Keywords: Key words Starch ; Wheat ; Starch synthase ; Gene structure ; Gene expression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  A cDNA clone, and a corresponding genomic DNA clone, containing full-length sequences encoding wheat starch synthase I, were isolated from a cDNA library of hexaploid wheat (Triticum aestivum) and a genomic DNA library of Triticum tauschii, respectively. The entire sequence of the starch synthase-I cDNA (wSSI-cDNA) is 2591 bp, and it encodes a polypeptide of 647 amino-acid residues that shows 81% and 61% identity to the amino-acid sequences of SSI-type starch synthases from rice and potato, respectively. In addition, the putative N-terminal amino-acid sequence of the encoded protein is identical to that determined for the N-terminal region of the 75-kDa starch synthase present in the starch granule of hexaploid wheat. Two prominent starch synthase activities were demonstrated to be present in the soluble fraction of wheat endosperm by activity staining of the non-denaturing PAGE gels. The most anodal band (wheat SSI) shows the highest staining intensity and results from the activity of a 75-kDa protein. The wheat SSI mRNA is expressed in the endosperm during the early to mid stages of wheat grain development but was not detected by Northern blotting in other tissues from the wheat plant. The gene encoding the wheat SSI (SsI-D1) consists of 15 exons and 14 introns, similar to the structure of the rice starch synthase-I gene. While the exons of wheat and rice are virtually identical in length, the wheat SsI-D1 gene has longer sequences in introns 1, 2, 4 and 10, and shorter sequences in introns 6, 11 and 14, than the corresponding rice gene.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s001220051186
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