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  • 11
    ISSN: 1434-4475
    Keywords: Ruthenium ; Binuclear complexes ; X-Ray analysis ; Oxidation ; Bisphosphines
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: Zusammenfassung Die Komplexe {RuCp*(μ-Cl)}2(μ-dppm) (1) und {RuCp*(μ-Cl2(μ-dppe) (3) wurden durch Umsetzung von [RuCp*(μ3-Cl)]4 mitdppm bzw.dppe dargestellt.1 wird durch AgCF3SO3 zum zweikernigen Komplex [{RuCp*(μ-Cl)}2(μ-dppm)](SO3CF3)2 (2) oxidiert, welcher eine Ru-Ru-Metallbindung aufweist. Unter den gleiche Reaktionsbedingungen zersetzt sich3 zu undefinierten Produkten. Analog zu1 reagiert RuCp* (dmpe)Cl mit AgCF3SO3 zum Ru(III)-Komplex [Ru(Cp*)(dmpe)Cl](SO3CF3) (4) wobei es zu keiner Chloridabspaltung kommt. Von2,3, und4 wurden die Kristallstrukturen bestimmt.
    Notes: Summary The dinuclear complexes {RuCp*(μ-Cl)}2(μ-dppm) (1) and {RuCp*(μ-Cl)}2 (μ-dppe) (3) are obtained by reacting [RuCp*(μ3-Cl)]4 withdppm, anddppe, respectively.1 is readily oxidized with AgCF3SO3, instead of chloride abstraction, to afford the dinuclear complex [{RuCp*(μ-Cl)}2(μ-dppm)](SO3CF3)2 (2) with two metal centers connected by a single Ru-Ru bond. Under the same conditions,3 decomposes to several intractable materials. Similarly to1, RuCp* (dmpe)Cl reacts with AgCF3SO3 to afford the Ru(III) complex [RuCp*(dmpe)Cl](SO3CF3) (4) without no halide abstraction. The crystal structures of2,3, and4 are presented.
    Type of Medium: Electronic Resource
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  • 12
    ISSN: 1432-1211
    Keywords: Key words NFKB2 ; p52 ; p100
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  NFKB2 is a member of the NFKB/Rel gene family, which is known to be a pivotal regulator of the acute phase and immune responses. NF-κB2 is initially synthesized as a ∼100 000 M r protein which needs to be processed in order to bind DNA, either as homodimer or as heterodimer with other members of the NF-κB/Rel family. The unprocessed form of NF-κB2 acts as an IκB-like protein. Therefore, NF-κB2 has a dual function. In this report we describe the genomic structure, expression pattern, and chromosomal localization of mouse NFKB2. Genomic clones were isolated, which span the entire gene of approximately 8.5 kilobases (kb) including 1.5 kb of the promoter region. Comparison to its human and avian homologues revealed a strong evolutionary conservation of the gene structure including the exon/intron borders, sequence, and position of the nuclear localization signal, the glycine-hinge region, and the ankyrin repeats. By fluorescence in situ hybridization, mouse NFKB2 was mapped to Chromosome (Chr) MMU 19C3-D2, which is homologous to human Chr 10q24, at which position the human NFKB2 was previously located. NFKB2 is ubiquitously expressed, highest in lymph nodes and thymus, underlining its role in the immune function.
    Type of Medium: Electronic Resource
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  • 13
    Electronic Resource
    Electronic Resource
    Springer
    Naturwissenschaften 52 (1965), S. 475-475 
    ISSN: 1432-1904
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 14
    Electronic Resource
    Electronic Resource
    Springer
    Archives of dermatological research 119 (1914), S. 304-307 
    ISSN: 1432-069X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 15
    Electronic Resource
    Electronic Resource
    Springer
    Monatsschrift Kinderheilkunde 145 (1997), S. 588-592 
    ISSN: 1433-0474
    Keywords: Schlüsselwörter Kongenitale myotone Dystrophie ; Curshmann-Steinert-Batten-Syndrom ; CTG-Trinukleotid-Sequenzwiederholung ; Dystrophia myotonica ; Facies myopathica ; Key words Congenital myotonia dystrophy ; Curshmann-Steinert-Batten-Syndrom ; CTG-Trinukleotid sequence repetition ; Distrophy myotonica ; Facies myopathica
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Summary The subject of this report is a newborn female, suffering from hypotonia and breathing difficulties, delivered in the 37 week with the help of forceps. Because of the nature of her symptons and those of the mother, which included Facies myopathica and Myotonia, the possibility of the expansion of a CTG-Trinukleotidsequence in the area of Chromosom 19 was explored. For this purpose a technique, developed in 1992, for the identification of molecular genetic characteristics was used. Instead of the 5 to 27 copies of the CTG sequence normally found in the population, the sick child had 1000 and the mother more than 700. EMG, in which a classical relases of myotones (Fall-Fight-Bomberscream) were found, confirmed the neurological diagnosis. Discussion: In the course of time the newborn child showed the classical problems of hyptotonia, such as respiratory difficulties, eating disorders leading to a loss of weight, meteroism, and after another stay in hospital, symptoms of Ileus.
    Notes: Zusammenfassung Es wird über ein in der 37. SSW durch Forzeps geborenes Mädchen berichtet, das durch Hypotonie und Ateminsuffizienz auffiel. Diese Symptome, ebenso wie die Facies myopathica und die Myotonie der Hand der Mutter bei der Begrüßung, gaben den Hinweis zur Durchführung der seit 1992 möglichen molekulargenetischen Bestimmung der Expansion einer CTG-Trinukleotidsequenz im Bereich des Chromosoms 19. Statt der in der Normalbevölkerung 5–27 Kopien dieser CTG-Sequenz-Wiederholung fanden sich bei dem erkrankten Kind über 1000 und bei der Mutter über 700. Darüber hinaus konnte durch eine neurologische Untersuchung der Mutter die bisher unbekannte Diagnose bestätigt werden, wobei im EMG eine klassische myotone Entladung (Sturz-Kampf-Bomber-Geräusch) gefunden wurde. Diskussion: Beim Neugeborenen traten im weiteren Verlauf die klassischen Folgeprobleme der Hypotonie wie Respiratorbedürftigkeit und Ernährungsprobleme mit relativer Gewichtsabnahme, Meteorismus und bei einer erneuten stationären Aufnahme Ileussymptomatik auf.
    Type of Medium: Electronic Resource
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  • 16
    Electronic Resource
    Electronic Resource
    Springer
    Applied microbiology and biotechnology 47 (1997), S. 502-507 
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Glucose oxidase from Penicillium amagasakiense was purified to homogeneity by ion-exchange chromatography and deglycosylated with endoglycosidase H. On the basis of gas chromatography and sodium dodecyl sulphate/polyacrylamide gel electrophoretic (SDS-PAGE) analyses, the protein-bound high-mannose-type carbohydrate moiety corresponded to 13% of the molecular mass of glycosylated glucose oxidase. A total of six N-glycosylation sites per dimer were determined from the N-acetylglucosamine content. The enzymatically deglycosylated enzyme contained less than 5% of the original carbohydrate moiety. A molecular mass of 130 kDa (gel filtration) and 133 kDa (native PAGE) was determined for the dimer and 67 kDa (SDS-PAGE) for the monomer of the deglycosylated enzyme. The N-terminal sequence, which has not been published for glucose oxidase from P. amagasakiense to date and which showed less than 50% homology to the N terminus of glucose oxidase from Aspergillus niger, and the amino acid composition were not altered by the deglycosylation. Deglycosylation also did not affect the kinetics of glucose oxidation or the pH and temperature optima. It also did not increase the susceptibility of the enzyme to proteolytic degradation. However, deglycosylated glucose oxidase exhibited decreased pH and thermal stability. The thermal stability of both enzymes was shown to be dependent on the buffer concentration and was enhanced by certain additives, particularly 1 M (NH4)2SO4, which stabilised glucose oxidase 100- to 300-fold at 50 °C and pH 7–8, and 2 M KF, which stabilised the enzyme up to 36-fold at 60 °C and pH 6. In sodium acetate buffer, changes in pH (4–6) affected the affinity for glucose but had no effect on the V max of the reaction. In contrast, in TRIS buffer, pH 8, a 10-fold decrease in V max and a 2-fold decrease in K m were observed.
    Type of Medium: Electronic Resource
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  • 17
    Electronic Resource
    Electronic Resource
    Springer
    Applied microbiology and biotechnology 49 (1998), S. 405-410 
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract An efficient expression system for the previously only weakly expressed thermophilic lipase BTL2 (Bacillus thermocatenulatus lipase 2) was developed for the production of large amounts of lipase in Escherichia coli. Therefore, the gene was subcloned in the pCYTEXP1 (pT1) expression vector downstream of the temperature-inducible λ promoter PL. Three different expression vectors were constructed: (i) pT1-BTL2 containing the mature lipase gene, (ii) pT1-preBTL2 containing the prelipase gene and (iii) pT1-OmpABTL2 containing the mature lipase gene fused to the signal peptide of the OmpA protein, the major outer membrane protein of E. coli. With pT1-BTL2 and pT1-preBTL2, comparable expression levels of 7000–9000 U/g cells were obtained independently of the E. coli host. In contrast, with E. coli JM105 harbouring pT1-OmpABTL2, 660 000 soluble lipase U/g cells was produced, whereas, with E. coli DH5α and BL321, production levels of 30 000 U/g cells were achieved. However, most of the lipase remained insoluble but active after cell breakage because of the unprocessed OmpA signal peptide. A simple cholate extraction followed by proteinase K cleavage and ultrafiltration allowed the isolation of 1.15 × 106 units of 90% pure mature lipase/wet cells.
    Type of Medium: Electronic Resource
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  • 18
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract A disposable-type microbial sensor was developed for the determination of both the biochemical oxygen demand for nitrification (N-BOD) and inhibiting effects on nitrifying bacteria. The sensor was based on the respiratory activity of nitrifying bacteria immobilized on a miniature oxygen electrode. Typical response times for measuring N-BOD of ammonium standard solutions as well as of wastewater samples were in the range of 6–12 min. A dynamic evaluation of the signals after a measuring time of 120 s also resulted in good reproducibility and sensitivity. A daily profile of a municipal sewage plant was recorded, comparing the biosensor data with two standard methods. For the measurement of nitrification-inhibiting effects a 120-s dynamic signal evaluation was preferred to a steady-state method because of the long recovery times resulting from extended exposure to inhibitors. However, steady-state measurement techniques allowed allylthiourea detection with a ten times higher sensitivity. Because of the advantages of this miniaturized electrode, e.g. short response time, simple measuring procedure and low costs of production, this sensor system is considered to be suitable for commercial application in environmental analysis.
    Type of Medium: Electronic Resource
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  • 19
    Electronic Resource
    Electronic Resource
    Springer
    Applied microbiology and biotechnology 45 (1996), S. 600-606 
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  Geotrichum candidum was found to produce a lactate oxidase. The enzyme was purified by gel filtration and ion-exchange chromatography. The purified lactate oxidase showed a molecular mass of 50 kDa under denaturing and about 400 kDa under non-denaturing conditions. Transmission electron micro-scopy analysis confirmed an octameric structure. FMN was found to be a cofactor for this enzyme. Polarographic studies confirmed an oxygen uptake by the lactate oxidase. The enzyme showed specificity towards the L isomer of lactate and did not oxidise pyruvate, fumarate, succinate, maleate and ascorbate. It was stable at alkaline pH and also for 15 min at 45°C. The addition of glycerol and dextran 500 000 to the enzyme sample enhanced storage stability.
    Type of Medium: Electronic Resource
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  • 20
    Electronic Resource
    Electronic Resource
    Oxford [u.a.] : International Union of Crystallography (IUCr)
    Acta crystallographica 51 (1995), S. 361-364 
    ISSN: 1600-5759
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Type of Medium: Electronic Resource
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