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  • 1
    Call number: QZ266.6:23
    Keywords: Thermotherapy ; Hyperthermia, Induced ; Tumor / Therapie
    Pages: ix, 84 p. : ill.
    ISBN: 3540545603
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  • 2
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Each of at least five unlinked MAL loci (MAL1 through MAL4 and MAL6) on the yeast genome controls the ability to synthesize an inducible α-D-glucosidase (maltase). A subcloned fragment of the coding sequence of the MAL6 maltase structural gene was used as a hybridization probe to investigate the physical structure of the family of MAL structural genes in the genomes of different Saccharomyces strains. Mal+ strains, each carrying a genetically defined MAL locus, were crossed with a Mal- strain and the segregation behavior of the functional locus and of sequences complementary to the maltase structural gene at that locus analyzed. The maltase structural gene sequences of each MAL locus were detected by Southern blot hybridization using BamH1 digests of genomic DNA of the meiotic products. This restriction enzyme was previously shown to cleave outside the confines of the MAL6 locus. The results of such experiments indicate that each MAL locus encompasses at least one maltase structural gene sequence homologous to that of MAL6, that yeast strains that lack functional MAL loci may or may not contain the corresponding maltase structural gene sequence, that the MAL1 maltase structural gene sequence or one of its alleles can be detected in all laboratory yeast strains examined and that each MAL locus can be identified as a characteristic BamH1 fragment of genomic DNA which includes a maltase structural gene. Yeast strains vary in the number of maltase structural gene sequences that they carry. By using the approach described in this report, the ones corresponding to the different functional MAL loci and residing within a BamH1 generated restriction fragment can be identified.
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  • 3
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The Escherichia coli Tn9 derived chloramphenicol resistance gene (cam r) is functionally expressed in the yeast Saccharomyces cerevisiae. This gene was introduced into yeast cells as part of a hybrid yeast/E. coli shuttle plasmid. A number of plasmid associated yeast mutants overproducing the cam r gene product, chloramphenicol acetyltransferase (acetyl-CoA: chloramphenicol 3-0-acetyltransferase, E.C. 2.3.1.28) were isolated. One of the plasmid mutants was analyzed in some detail. Even though this mutant showed a 1,000 fold overproduction of chloramphenicol acetyltransferase in the yeast host the level of RNA complementary to the cam r gene was not increased. A deletion of 127 base pairs in the region immediately upstream from the 5′ end of the cam r gene appeared to be responsible for the “up” phenotype of this mutant. This mutation affected the expression of the cam r gene in E. coli in a “down” fashion, in contrast to its effect in yeast.
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  • 4
    ISSN: 1617-4623
    Keywords: Key words Hydrolase ; Enterobacter ; Amidohydrolase Carboxypeptidase ; Indole-3-acetylaspartic acid
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A 5.5-kb DNA fragment containing the indole-3-acetyl-aspartic acid (IAA-asp) hydrolase gene (iaaspH) was isolated from Enterobacter agglomerans strain GK12 using a hybridization probe based on the N-terminal amino acid sequence of the protein. The DNA sequence of a 2.4-kb region of this fragment was determined and revealed a 1311-nucleotide ORF large enough to encode the 45-kDa IAA-asp hydrolase. A 1.5-kb DNA fragment containing iaaspH was subcloned into the Escherichia coli expression plasmid pTTQ8 to yield plasmid pJCC2. Extracts of IPTG-induced E. coli cultures containing the pJCC2 recombinant plasmid showed IAA-asp hydrolase levels 5 to 10-fold higher than those in E. agglomerans extracts. Homology searches revealed that the IAA-asp hydrolase was similar to a variety of amidohydrolases. In addition, IAA-asp hydrolase showed 70% sequence identity to a putative thermostable carboxypeptidase of E. coli.
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  • 5
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Fermentation of maltose by Saccharomyces strains depends on the presence of any one of five unlinked MAL loci (MAL1, MAL2, MAL3, MAL4 or MAL6). Earlier mutational analyses of MAL2 and MAL6 containing strains have identified a single complementation group at each of these two loci. However complementation analysis between naturally occurring Mal− Saccharomyces strains isolated from the wild demonstrated the presence of two complementation groups (designated MALp and MALg) at the MAL1, MAL3 and MAL6 loci. The available evidence suggests that the MALp gene is functionally equivalent to the complementation group identified by mutational analysis at the MAL6 locus and that this gene encodes a protein involved in the regulation of the coordinate induction of both maltase and maltose permease synthesis. In this paper we report the isolation, in a well characterized MAL1 strain, of 47 mutants unable to ferment maltose. All the mutants, with one exception, map at the MAL1 locus. These mal1 mutants, except for one, are recessive to MAL1 and fall into two major complementation groups. Evidence is presented that these two classes of mutants identify both a gene involved in the regulation of maltose fermentation (MAL1R) and a gene involved in maltose transport (MAL1T). We also report here the isolation of a temperature sensitive maltose nonfermenting mutant mapping at the MAL1 locus identifying a third gene (MAL1S) at this locus. The maltase synthesized by this mutant, when assayed in cell-free extracts, is significantly more thermolabile than the wild type enzyme. Our findings demonstrate that MAL1 is a complex locus comprising at least three genes: MAL1R, a gene involved in the coordinate regulation of the synthesis of maltase and maltose transport; MAL1T, a gene encoding a component of the maltose transport system; and MAL1S, a likely candidate for the structural gene for maltase.
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  • 6
    Electronic Resource
    Electronic Resource
    Oxford [u.a.] : International Union of Crystallography (IUCr)
    Acta crystallographica 52 (1996), S. 2832-2835 
    ISSN: 1600-5759
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
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  • 7
    ISSN: 1600-5740
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: As part of the molecular recognition studies on the phytohormone indole-3-acetic acid (IAA) a series of fluorinated IAA's has been examined. The phenyl ring substitution at positions 4, 5, 6 and 7 resulted in four compounds, which were analyzed. Structure–activity correlation includes the analysis of their molecular conformations, based on the X-ray diffraction and computational chemistry results, and bioactivity determinations in the Avena coleoptile and the Pisum sativum stem straight-growth tests, lipophilicity and UV absorbance. The conformations of monofluorinated IAA's and a free hormone are defined by rotations about two bonds: one describes the relative orientation of a side chain towards the indole plane and the second the orientation of the carboxylic group. The results of X-ray structure analysis revealed the folded shape of the molecules in all compounds studied. Molecular mechanics and dynamics located the folded conformation as the local minimum, but failed to detect the planar conformation as one of the local minima, which according to ab initio results on IAA and 4-CI-IAA could also be possible. Crystal data at 295 K for 4-F-IAA and at 297 K for 5-F-IAA, and at 100 K for 6-F-IAA and 7-F-IAA using Mo Kα radiation (λ = 0.71073 Å) and Cu Kα (λ = 1.5418 Å, for 7-F-IAA), are as follows: 4-F-IAA, C10H8NO2F, Mr = 193.18, monoclinic, C2/c, a = 17.294 (5), b = 13.875 (4), c = 7.442 (4) Å, β = 103.88 (6)°, V = 1734 (1) Å3, Z = 8, Dx = 1.480 g cm−3, μ = 1.1 cm−1, F(000) = 800, R = 0.043, wR = 0.044 for 823 symmetry-independent [I ≥ 3σ(I)] reflections; 5-F-IAA, C10H8NO2F, monoclinic, P21/c, a = 19.284 (5), b = 5.083 (4), c = 9.939 (4) Å, β = 117.28 (6)°, V = 865.9 (1) Å3, Z = 4, Dx = 1.482 g cm−3, μ = 1.1 cm−1, F(000) = 400, R = 0.062, wR = 0.057 for 729 symmetry-independent [I ≥ 3σ(I)] reflections; 6-F-IAA, C10H8NO2F, monoclinic, P21/a, a = 9.360 (1), b = 5.167 (4), c = 17.751 (4) Å, β = 93.75 (1)°, V = 856.7 (8) Å3, Z = 4, Dx = 1.498 g cm−3, μ = 1.1 cm−1, F(000) = 400, R = 0.048, wR = 0.048 for 1032 symmetry-independent [I ≥ 2σ(I)] reflections; 7-F-IAA, C10H8NO2F, monoclinic, P21/a, a = 9.935 (5), b = 5.0059 (4), c = 17.610 (1) Å, β = 102.13 (1)°, V = 856.3 (1) Å3, Z = 4, Dx = 1.498 g cm−3, μ = 9.8 cm−1 (Cu Kα, F(000) = 400, R = 0.035, wR = 0.040 for 1504 symmetry-independent [I ≥ 2σ(I)] reflections.
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  • 8
    ISSN: 1600-5740
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The physiological properties of the phytohormone (auxin) indole-3-acetic acid (IAA) and its ring substituted derivatives have so far been rationalized by a number of contradictory hypotheses based on incomplete structural data deduced mainly by inspection of molecular models. In order to give more evidence for structure–activity relationships of monohalogenated IAA's, the molecular structures of the natural auxin 4-CI-IAA as well as 5-CI-IAA, 6-CI-IAA, 7-CI-IAA and 5-Br-IAA have been compared, as revealed by X-ray analysis, and molecular mechanics and dynamics. The influence of the substitution site and the size of the halogen atom and bioactivity is discussed. The typical structural feature of the molecules studied is the slight distortion of part of the indole nucleus around C7: bond length C6—C7 1.368 (6) Å and C6—C7—C71 117.6 (3)° (average values of five structures and seven molecules). The conformations of monohalogenated indole-3-acetic acid molecules, characteristic for auxins, are defined by rotations about two bonds only: one describes the relative orientation of a side chain towards the indole moiety and the second the orientation of the carboxylic group. The results of X-ray structure analysis, and molecular mechanics and dynamics revealed the folded shape of the molecules in all compounds studied. Ab initio calculations showed that the planar conformation can be adopted as well. Crystal data at 297 K for 4-CI-IAA, 6-CI-IAA, 7-CI-IAA and 5-Br-IAA, and at 220 K for 5-CI-IAA, using Mo Kα radiation (λ = 0.71073 Å), and CuKα (λ = 1.5418 Å) for 6-CI-IAA, are as follows: 4-CI-IAA, C10H8ClNO2, Mr = 209.63, monoclinic, P21/c, a = 7.313 (4), b = 17.156 (4), c = 7.640 (4) Å, β = 92.71 (5)°, V = 957.5 (1) Å3, Z = 4, Dx = 1.454 g cm−3, μ = 3.7 cm−1, F(000) = 432, R = 0.037, wR = 0.039 for 1040 symmetry-independent [I ≥ 3σ(I)] reflections; 5-CI-IAA, C10H8ClNO2, monoclinic, P21/c, a = 19.141 (4), b = 5.154 (2), c = 10.323 (3) Å, β = 116.23 (2)°, V = 913.5 (1) Å3, Z = 4, Dx = 1.524 g cm−3, μ = 3.8 cm−1, F(000) = 432, R = 0.039, wR = 0.042 for 1184 symmetry-independent [I≥ 3σ(I)] reflections; 6-CI-IAA, C10H8ClNO2, orthorhombic, Pbca, a = 61.08 (1), b = 12.115 (7), c = 7.674 (5) Å, V = 5679 (5) Å3, Z = 24, Dx = 1.471 g cm−3, μ = 33.9 cm−1, F(000) = 2592, R = 0.052, wR = 0.052 for 3030 symmetry-independent [I ≥ σ(I)] reflections; 7-CI-IAA, C10H8ClNO2, monoclinic, P21/c, a = 20.244 (5), b = 4.829 (2), c = 10.728 (4) Å, β = 116.30 (1)°, V = 940 (1) Å3, Z = 4, Dx = 1.481 g cm−3, μ = 3.7 cm−1, F(000) = 432, R = 0.042, wR = 0.029 for 889 symmetry-independent [I ≥ 3σ(I)] reflections; 5-Br-IAA, C10H8BrNO2, Mr = 254.08, triclinic, P{\bar 1}, a = 5.645 (3), b = 9.713 (4), c = 10.019 (4) Å, α = 116.02 (3), β = 92.67 (5), γ = 100.12 (4)°, V = 481.2 (5) Å3, Z = 2, Dx = 1.754 g cm−3, μ = 42.0 cm−1, F(000) = 252, R = 0.029, wR = 0.020 for 1865 symmetry-independent [I ≥ 3σ(I)] reflections.
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  • 9
    ISSN: 1365-2044
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: A previously healthy young male developed unilateral pulmonary oedema immediately after re-expansion of an intentionally collapsed lung after transaxillary sympathectomy. The pulmonary oedema was localised to the contralateral, uncollapsed lung.
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  • 10
    ISSN: 1365-2133
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
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