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  • Springer  (35)
  • Springer Nature  (7)
  • American Physical Society  (2)
  • Institute of Physics  (2)
  • 1
    Digitale Medien
    Digitale Medien
    Springer
    The European physical journal 321 (1985), S. 221-223 
    ISSN: 1434-601X
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Physik
    Notizen: Abstract Energy loss of slow protons in a degenerate electron gas is calculated on the basis of the dielectric theory. The influence of static and dynamic local field corrections is examined. Comparison with well defined experimental data is made.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    ISSN: 1432-0614
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Notizen: Summary Biotransformations were developed to oxidize Nε-carbobenzoxy(CBZ)-l-lysine and to reduce the product keto acid to l-CBZ-oxylysine. Lysyl oxidase (l-lysine: O2 oxidoreductase, EC 1.4.3.14) from Trichoderma viride was relatively specific for l-lysine and had very low activity with Nε-substituted derivatives. l-Amino acid oxidase (l-amino acid: O2 oxidoreductase [deaminating], EC 1.4.3.2) from Crotalus adamanteus venom had low activity with l-lysine but high activity with Nε-formyl-, t-butyoxycarbonyl(BOC)-, acetyl-, trifluoroacetyl-, or CBZ-l-lysine. l-2-Hydroxyisocaproate dehydrogenase (EC 1.1.1.-) from Lactobacillus confusus catalyzed the reduction by NADH of the keto acids from Nε-acetyl-, trifluoroacetyl-, formyl- and CBZ-l-lysine but was inactive with the products from oxidation of l-lysine, l-lysine methyl ester, l-lysine ethyl ester or Nε-t-BOC-l-lysine. Providencia alcalifaciens (SC9036, ATCC 13159) was a good microbial substitute for the snake venom oxidase and also provided catalase (H2O2:H2O2 oxidoreductase EC 1.11.1.6). Nε-CBZ-l-Lysine was converted to CBZ-l-oxylysine in 95% yield with 98.5% optical purity by oxidation using P. alcalifaciens cells followed by reduction of the keto acid using l-2-hydroxyisocaproate dehydrogenase. NADH was regenerated using formate dehydrogenase (formate: NAD oxidoreductase, EC 1.2.1.2) from Candida boidinii. The Providencia oxidase was localized in the particulate fraction and catalase activity was predominantly in the soluble fraction of sonicated cells. The pH optima and kinetic constants were determined for the reactions.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 3
    Digitale Medien
    Digitale Medien
    Springer
    Microchimica acta 73 (1980), S. 277-287 
    ISSN: 1436-5073
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Chemie und Pharmazie
    Beschreibung / Inhaltsverzeichnis: Zusammenfassung Molybdat bildet mit Brenzcatechinviolett in schwach saurer Lösung einen 1∶1-Komplex. Bei dem optimalen pH 2,7 beträgt die scheinbare Stabilitätskonstante (1,52 ±0,12)×104l·mol−1 und die molare Extinktion bei 540 nm 2,70×104l·mol−1·cm−1. Bei höherem oder niedrigerem pH nimmt die Stabilität des Komplexes ab. Im pH-Gebiet 2–5 bildet Molybdat mit Alizarinrot S einen 1∶2-Komplex. Dessen scheinbare Stabilitätskonstante beträgt (4,8±0,6)× 107l·mol−1 bei dem optimalen pH=3,8 und die molare Extinktion (9,30± 0,30)×103l·mol−1·cm−1 bei 480 nm. In 0,1M saurer Lösung existiert ein weniger stabiler 1∶1-Komplex, dessen logK=4,2. Beide Farbstoffe eignen sich für die Bestimmung von Molybdat in schwach oder stark saurer Lösung. In der Nähe des isoelektrischen Punktes der Molybdänsäure (pH 1,5-2,0) können genaue Analysenergebnisse nur erhalten werden, wenn die Molybdatlösung vorher neutralisiert und 10 min gekocht wird, um die weniger reaktionsfähigen polymeren Formen des Molybdäns abzubauen. Es wird angenommen, daß Mo(OH)6 die hexakoordinierte reaktionsfähige Form darstellt, die mit den Polyphenolen Ester bildet.
    Notizen: Summary Molybdate forms a 1∶1 complex with Pyrocatechol Violet in weakly acidic solutions. At the optimum pH 2.7 the apparent stability constant is (1.52±0.12)×104l·mole−1 and the molar absorptivity 2.70×104l·mole−1·cm−1 at 540 nm. At higher and lower pH the stability of the complex decreases. In the pH range 2–5 molybdate forms a 1∶2 complex with Alizarin Red S. The apparent stability constant is (4.8±0.6)×107l·mole−1 at the optimum pH 3.8 and the molar absorptivity (9.30±0.30)×103l· mole−1·cm−1 at 480 nm. In 0.1M acid solution a less stablel: 1 complex exists, logK=4.2. Both dyes are appropriate reagents for estimation of molybdate when present in weakly or strongly acidic solutions. Near to the isoelectric point of molybdic acid (pH 1.5–2.0) accurate analysis data can be obtained only when the molybdate solution to be analysed is neutralized and boiled for 10 min to transform the less reactive polymeric molybdenum species. It is thought that hexacoordinated Mo(OH)6 is the reactive species, forming esters with the polyphenols used.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 4
    ISSN: 1432-0614
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Notizen: Summary A key chiral intermediate lactol(3)[3aS (3aα,4α,7α,7aα)]-hexahydro-4,7-epoxy-isobenzofuran-1 (3H)-one was prepared for the total synthesis of a new thromboxane antagonist. The stereoselective hydrolysis of (exo,exo)-7-oxabicyclo[2.2.1]heptane-2,3-dimethanol, diacetate ester (1) to the corresponding chiral monoacetate ester (2) was carried out with lipases, among which Amano P-30 lipase from Pseudomonas sp. was most effective since it gave the desired enantiomer of monoacetate ester. A yield of 75 mol% and optical purity of 〉99% was obtained when the reaction was conducted in a biphasic system with 10% toluene at 5 g/l of the substrate. Lipase P-30 was immobilized on Accurel polypropylene (PP) and the immobilized enzyme was reused (five cycles) without loss of enzyme activity, productivity or optical purity. The reaction process was scaled-up to 80 1 (400 g substrate) and monoacetate (2) was isolated in 80 mol% yield with 99.3% optical purity as determined by chiral HPLC and nuclear magnetic resonance (NMR) analysis. A gas chromatography of 99.5% and specific rotation, [α]D of -7.6° was obtained. The chiral monoacetate ester (2) was oxidized to its corresponding aldehyde and subsequently hydrolyzed to give lactol (3).
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 5
    Digitale Medien
    Digitale Medien
    Springer
    Applied microbiology and biotechnology 36 (1991), S. 29-34 
    ISSN: 1432-0614
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Notizen: Summary A key intermediate, S-(−)-3-benzoylthio-2-methylpropanoic acid (1) was made in high optical purity by the lipase-catalyzed stereoselective esterification of racemic 1 with methanol in an organic solvent system. Among various lipases evaluated, Amano P-30 lipase from Pseudomonas sp. efficiently catalyzed the esterification of 1 to yield R-(+) methyl ester and unreacted S-(−) 1. A reaction yield of 40 mol% and an optical purity of 97.2% were obtained for compound 1 at a substrate concentration of 0.1 m (22 mg/ml). Lipase P-30 was immobilized on Accurel polypropylene (PP) and the immobilized enzyme was reused (23 cycles) in the esterification reaction without loss of enzyme acitivity, productivity or optical purity. Among various solvents evaluated, toluene was found to be the most suitable organic solvent and methanol was the best alcohol for the esterification of racemic 1 by immobilized lipase. Substrate concentrations as high as 1.0 m were used in the esterification reaction. When the temperature was increased from 28° C to 60° C, the reaction time required for the esterification of 0.1 m substrate decreased from 16 h to 2 h. On increasing the methanol to substrate molar ratio from 1:1 to 4:1, the rate of esterification decreased. A lipase fermentation using Pseudomonas sp. ATCC 21 808 was developed. In the batch-fermentation process, 56 units/ml of extracellular lipase activity was obtained. A fed-batch process using soybean oil gave a significant increase in the lipase activity (126 units/ml). Crude lipase recovered from the filtrate by ethanol precipitation and immobilized on Accurel PP was also effective: S-(−) compound 1 was obtained in 35 mol% yield and 95% optical purity.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 6
    ISSN: 1432-0614
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Notizen: Summary A chiral compound [4R-[4α,6ß(E)]]-6-[4,4-bis(4-fluorophenyl)-3-(1-methyl-1H-tetrazol-5-yl)-1,3-butadienyl]-tetrahydro-4-hydroxy-2H-pyran-2-one (R-(+)-1) was prepared by the lipase-catalysed stereoselective acetylation of racemic 1 in an organic solvent. Chiral R-(+)-1 is a hydroxymethyl glutaryl coenzyme A (HMG CoA) reductase inhibitor and a potential anticholesterol drug candidate. Among various lipases evaluated, lipase PS-30 from Pseudomonas species efficiently catalysed acetylation of the undesired enantiomer of racemic 1 to yield the S-(−)-acetylated product 2 and unreacted desired R-(+)-1. A reaction yield of 48 mol% and an optical purity of 98% were obtained for R-(+)-1 when the reaction was conducted in toluence as solvent in the presence of isopropenyl acetate as acyl donor. Lipase PS-30 was immobilized on Accurel polypropylene (PP) and the immobilized enzyme was reused (five cycles) in the acetylation reaction without loss of enzyme activity, productivity, or optical purity of the R-(+)-1. The enzymatic acetylation process was scaled-up to 501 and a 640-l volume (preparative batches) at a substrate concentration of 4 g/l. R-(+)–1 was recovered from the preparative batches in 68–71% recovery yield with 98.5% gas chromatography homogeneity index and 98.5% optical purity. The S-(−) acetate 2 produced by the acetylation reaction was enzymatically hydrolysed by lipase PS-30 in a biphasic system to prepare the corresponding S-(−)-1.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 7
    Digitale Medien
    Digitale Medien
    Springer
    Applied microbiology and biotechnology 40 (1993), S. 241-245 
    ISSN: 1432-0614
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Notizen: Abstract Several microbial cultures were screened for the ability to catalyse the reduction of N-(4-(1-oxo-2-chloroacetyl ethyl) phenyl methane sulfonamide (1). The chiral intermediate (+)N-(4-(1-hydroxy-2-chloroethyl) phenyl methane sulfonamide (2) was prepared by the stereoselective microbial reduction of the parent ketone 1. Compound 2 is a potential chiral intermediate for synthesis of 4-(2-isopropylamino-1-hydroxyethyl) phenyl methanesulfonanilide (d-sotalol), a beta-receptor antagonist. Microorganisms from the genera Rhodococcus, Nocardia, and Hansenula reduced 1 to 2. A reaction yield of 〉50% and optical purities of 〉90% were obtained. The best strain (H.polymorpha ATCC 26012) effectively reduced compound 1 to compound 2 in 95% reaction yield and 99% optical purity. Compound 2 (8.2 g) was isolated from a 3-1 preparative batch in 68% overall yield. Isolated compound 2 had a specific rotation of +20° (CH2Cl2, C-1), an optical purity of 99.5%, and a chemical purity of 97% as analyzed by gas chromatography and HPLC. The nuclear magnetic resonance and mass spectra of compound 2 prepared by bioreduction and a standard chemical sample of 2 were virtually identical. Cell extracts of H. polymorpha in the presence of glucose dehydrogenase, glucose and nicotinamide adenine dinucleotide (NAD +) catalyzed the reduction of 1 to 2 with 98% reaction yield and resulted in an optical purity of 99.4%.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 8
    Digitale Medien
    Digitale Medien
    Springer
    Applied physics 31 (1983), S. 153-155 
    ISSN: 1432-0630
    Schlagwort(e): 34.79
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Maschinenbau , Physik
    Notizen: Abstract The dependence on the bombarding energy of the number of ejected electrons from a policrystalline Ag target is determined. Statistical methods are used in the calculation of the inelastic energy loss due to binary atomic collisions and in that of the electronic stopping cross-section. The calculation is executed for the case of Se+ bombarding ion in the 10–200 keV energy range.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 9
    Digitale Medien
    Digitale Medien
    Springer
    Applied microbiology and biotechnology 34 (1990), S. 10-14 
    ISSN: 1432-0614
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Notizen: Summary A key intermediate (S(−) 2-cyclohexyl-1,3-propanediol monoacetate) was made with high optical purity for the total synthesis of a new angiotensin converting enzyme inhibitor, Fosinopril. The stereoselective hydrolysis of 2-cyclohexyl-1,3-propanediol diacetate (I) and 2-phenyl-1,3-propanediol diacetate (II) was carried out with lipases. Among various lipases evaluated, only porcine pancreatic lipase (PPL) and Chromobacterium viscosum lipase demonstrated efficient conversion and gave the desired enantiomer of monoacetate. In aqueous solution, the desired S(−) monoacetate exhibited an optical purity of 65%–80% (30%–60% enantiomeric excess [e.e.]). However, when the same reactions were conducted in a biphasic system, the product S(−) monoacetate exhibited an optical purity of 99%–100% (98%–100% e.e.). The high purity product was achieved with 65 mol% yield at 1% substrate concentration. Among various solvents evaluated in biphasic systems, efficient hydrolysis was achieved in toluene, cyclohexane, and trichloro-trifluoroethane. The crude PPL was partially purified and two lipase fractions (A and B) were identified. Lipases A and B had a molecular mass of 38 000 and 40 000 daltons, respectively, and both were found to catalyze the hydrolysis of I and II to the appropriate monoacetate in a biphasic system.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 10
    Digitale Medien
    Digitale Medien
    Springer
    Cellular and molecular life sciences 23 (1967), S. 84-85 
    ISSN: 1420-9071
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Medizin
    Notizen: Summary The inhibitory action ofHepatitis infectiosa virus on the SDH activity of Detroit-6 (VA) cell lines was investigated. The full inhibition of the SDH activity took place at the end of the third day after the infection. As this phenomenon precedes the cytopathogenetic effect of viral infection, it may be of some help in the early detection of the infection.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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