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  • Chemistry  (5)
  • Saccharomyces cerevisiae  (4)
  • Mla locus  (2)
  • 1990-1994  (5)
  • 1985-1989  (4)
  • 1950-1954  (1)
  • 1910-1914  (1)
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Year
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Current genetics 23 (1993), S. 375-381 
    ISSN: 1432-0983
    Keywords: Saccharomyces cerevisiae ; Isocitrate lyase ; Gene regulation ; Ethanol induction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The ICL1 gene encoding the isocitrate lyase from Saccharomyces cerevisiae was cloned and sequenced. A reading frame of 557 amino acids showing significant similarity to isocitrate lyases from seven other species could be identified. Construction of icl1 null mutants led to growth defects on C2 carbon sources while utilization of sugars or C3 substrates remained unaffected. Using an ICL1-lacZ fusion integrated at the ICL1 locus, a more than 200-fold induction of β-galactosidase activity was observed after growth on ethanol when compared with glucose-repressed conditions. A preliminary analysis of the ICL1 upstream region identified a 364-bp fragment necessary and sufficient for this regulatory phenotype. Sequence motifs also present in the upstream regions of co-regulated genes were found within this region.
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  • 2
    ISSN: 1432-0983
    Keywords: Saccharomyces cerevisiae ; Fructose-1,6-bisphosphatase ; Glucose repression ; Gene activation ; Gluconeogenesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Fructose-1,6-bisphosphatase is a key enzyme in gluconeogenesis and the FBP1 gene is not transcribed during growth with glucose. Genetic analysis indicated a positive regulation of FBP1 expression after exhaustion of glucose. By linker-deletion analysis, two upstream activation sites (UAS1 and UAS2) were localized and the respective UAS-binding factors (DAP I and DAP II for derepression activating protein) were identified by gel retardation. UAS1 and UAS2 span about 30 bp each, and are separated by approximately 30 bp. Both UAS sites act synergistically. Although UAS1 showed some similarities to the DNA-binding consensus for the general yeast activator Rap1, competition experiments and DEAE-chromatography proved that DAP I and Rap1 correspond to different proteins. Gel retardation by DAP I depended on carbon sources and did not occur in cells growing logarithmically with glucose, whereas a strong retardation signal was obtained with ethanol-grown cells. The present results suggest that DAP I and DAP II are the final regulatory elements for glucose derepression.
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Theoretical and applied genetics 85 (1993), S. 713-718 
    ISSN: 1432-2242
    Keywords: Barley ; Multigene family ; Mla locus ; Recombination ; RFLP marker
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The complex structure of the multigene family at the Mla locus conferring powdery mildew resistance in barley was studied by making diallel crosses between several near-isogenic lines carrying different Mla alleles. The mode of inheritance of the Mla alleles investigated was determined to be dominant for Mla1, Mla6, Mla7 and Mla13 and semidominant for Mla3, Mla12 and Mla20. F1 plants were backcrossed to the susceptible recurrent parent in order to identify susceptible and double-resistant recombinants in the BC1F1 generation. Out of 17605 progenies tested in the BC1F1 generation, two susceptible recombinants, one between Mla1 and Mla12 and one between Mla13 and Mla20 were confirmed. The former was also verified by RFLP analysis.
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Theoretical and applied genetics 84 (1992), S. 330-338 
    ISSN: 1432-2242
    Keywords: RFLP marker ; Barley ; Powdery mildew ; Mla locus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary To identify the mildew resistance locus Mla in barley with molecular markers, closely linked genomic RFLP clones were selected with the help of near-isogenic lines having the ‘Pallas’ and ‘Siri’ background. Out of 22 polymorphic clones 3 were located around the Mla locus on chromosome 5 with a distance of 5.1 + 2.9 cM (MWG 1H068), 4.2±1.7 cM (MWG 1H060) and 0.7 ± 0.7 cM (MWG 1H036), respectively. The polymorphic clone MWG 1H036 displayed the same RFLP pattern in both ‘Pallas’ and ‘Siri’ near-isogenic lines and in different varieties digested with six restriction enzymes possessing the same mildew resistance gene. The alleles of the Mla locus were grouped in 11 classes according to their specific RFLP patterns; 3 of these groups contain the majority of Mla alleles already used in barley breeding programs in Europe.
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  • 5
    ISSN: 1617-4623
    Keywords: Glucose repression ; Glucose derepression ; Regulatory genes ; Expression analysis ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Yeast strains carrying one of the two regulatory mutations cat1 and cat3 are defectve in derepression of several glucose-repressible enzymes that are necessary for utilizing non-fermentable carbon sources. Hence, these strains fail to grow on ethanol, glycerol or acetate. The synthesis of isocitrate lyase, malate synthase, malate dehydrogenase and fructose-1,6-bisphosphatase is strongly affected in cat1 and cat3 strains. Genes CAT1 and CAT3 have been isolated by complementation of the cognate, mutations after transformation with an episomal plasmid gene library. The restriction map of CAT1 proved its allelism to the earlier isolated SNF1 gene. Both genes appear to exist as single-copy genes per haploid genome as indicated by Southern hybridization. Northern analysis has shown that the 1.35 kb CAT3 mRNA is constitutively expressed, independent of the carbon source in the medium. Derepression studies with CAT3 transformants using a multi-copy plasmid showed over-expression of glyoxylate cycle enzymes. This result would be consistent with a direct effector function for the CAT3 gene product.
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  • 6
    ISSN: 1617-4623
    Keywords: GC clusters ; Mobile elements ; Target sites ; mtDNA ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary GC clusters constitute the major repetitive elements in the mitochondrial (mt) genome of the yeast Saccharomyces cerevisiae. Many of these clusters are optional and thus contribute much to the polymorphism of yeast mtDNAs. We have made a systematic search for polymorphic sites by comparing mtDNA sequences of various yeast strains. Most of the 26 di- or polymorphic sites found differ by the presence or absence of a GC cluster of the majority class, here referred to as the M class, which terminate with an AGGAG motif. Comparison of sequences with and without the GC clusters reveal that elements of the subclasses M1 and M2 are inserted 3′ to a TAG, flanked by A+T rich sequences. M3 elements, in contrast, only occur in tandem arrays of two to four GC clusters; they are consistently inserted 3′ to the AGGAG terminal sequence of a preexisting cluster. The TAG or the terminal AGGAG, therefore, are regarded as being part of the target sites for M1 and M2 or M3 elements, respectively. The dinucleotide AG is in common to both target sites; it also occurs at the 3′ terminus (AGGAG). This suggests its duplication during GC cluster insertion. This notion is supported by the observation that GC clusters of the minor classes G and V similarily repeat at their 3′ terminus a GT or an AA dinucleotide, respectively, from their putative target sites.
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  • 7
    ISSN: 1052-9306
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A specific and sensitive gas chromatographic/mass spectrometric method was developed and validated for the determination of the antidepressant levoprotiline in blood, plasma and urine and the simultaneous determination of levoprotiline and its desmethyl metabolite in urine. Deuterium-labelled analogues were used as internal standards. The compounds were isolated from the biological fluids by liquid-liquid extraction under basic conditions. Following derivatization with perfluoropropionic anhydride, the samples were analysed by capillary column gas chroma-tography/electron impact mass spectrometry with selected ion monitoring. The analysis of spiked samples demonstrated the high accuracy and precision of the method. Blood concentrations of levoprotiline down to 0.7 nmol I-1 (1 ml used for analysis) could be quantified with a coefficient of variation of 10% or less. The method is suitable for use in pharmacokinetic and bioavailability studies of levoprotiline in humans.
    Additional Material: 6 Ill.
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  • 8
    Electronic Resource
    Electronic Resource
    Weinheim [u.a.] : Wiley-Blackwell
    Materials and Corrosion/Werkstoffe und Korrosion 1 (1950), S. 430-430 
    ISSN: 0947-5117
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Liebigs Annalen 1987 (1987), S. 249-258 
    ISSN: 0170-2041
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: Building Units of Oligosaccharides, LXXVIII. - Synthesis of KDO-Containing Lipid A AnaloguesThe non-neighbouring group supported glycosidation of 12 with the suitably protected glycosyl bromide 9 of 2-azido-2-deoxy-D-glucose leads - in the presence of a heterogeneous silver catalyst - to the formation of the β-(1→6)-glycosidically linked disaccharide 14. It consists of two 2-azido-2-deoxy-D-glucose units. Partial deblocking of 14 furnishes 15. On glycosidation with KDO bromide this compound yields the trisaccharide 16, which contains a KDO unit in an α-(2→6) ketosidic bond. Reduction of the two azido groups followed by amidation with (R)-3-hydroxymyristic acid and further deblocking generates the trisaccharide α-KDO-(2→6)-β-D-GlcA-(1→6)-D-GlcA 20 with two 3-hydroxy fatty acid residues in an amidic linkage.
    Notes: Die Umsetzung des Pyranosylbromids 9 der 2-Azido-2-desoxy-D-glucose mit dem Akzeptor 12 führt bei Gegenwart eines heterogenen Silberkatalysators ohne Nachbargruppenbeteiligung unter Inversion zum β-(1→6)-glycosidisch verknüpften Disaccharid 14 aus zwei 2-Azido-2-desoxy-D-glucose-Einheiten. Nach partieller Entblockierung zu 15 ist die Anknüpfung eines KDO-Restes unter Bildung einer α-(2→6)-ketosidischen Bindung zum Trisaccharid 16 möglich. Nach Reduktion der Azidogruppen und Anknüpfung von (R)-3-Hydroxymyristinsäure-Resten gelangt man nach Entblockierung zum Trisaccharid α-KDO-(2→6)-β-D-GlcA-(1→6)-D-GlcA 20, das amidartig zwei 3-Hydroxyfettsäure-Reste gebunden enthält.
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  • 10
    ISSN: 0170-2041
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: Branched and Chain-extended Sugars, XXX.  -  Diastereoselective Synthesis of L-glycero-D-manno-Heptose, a Constituent of the Inner Core Region of LipopolysaccharidesReaction of 2,3;5,6-di-O-isopropylidene-D-mannofuranose (1) with 2-lithio-1,3-dithiane affords diastereoselectively the 3,4;6,7-di-O-isopropylidene-D-glycero-D-galacto-heptose trimethylene dithioacetal (3). Conversion of compound 3 by a sequence of steps gives the tri-O-isopropylidene-D-glycero-D-galacto-heptit 16 which is oxidized with 1,1′-(azodicarbonyl)-dipiperidine to give the tri-O-isopropylidene-L-glycero-D-manno-heptose 17. Finally, compound 17 is transferred via the acetate 19 into the L-glycero-D-manno-heptopyranose 18.
    Notes: 2,3;5,6-Di-O-isopropyliden-D-mannofuranose (1) reagiert diastereoselektiv mit 2-Lithio-1,3-dithian zum 3,4;6,7-Di-O-isopropyliden-D-glycero-D-galacto-heptose-trimethylendithioacetal (3). Nach Umwandlung von 3 über eine Reihe von Zwischenstufen zum Tri-O-isopropyliden-D-glycero-D-galacto-heptit 16 läßt sich dieser mit 1,1′-(Azodicarbonyl)dipiperidin zur Tri-O-isopropyliden-L-glycero-D-manno-heptose 17 oxidieren. Hieraus ist über das Acetat 19 die freie L-glycero-D-manno-heptopyranose 18 zu gewinnen.
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