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  • 1
    ISSN: 1432-072X
    Keywords: Pyrimidine biosynthesis ; Aspartate transcarbamoylase ; Pyrimidine auxotroph ; Pseudomonas pseudoalcaligenes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The five de novo enzyme activities unique to the pyrimidine biosynthetic pathway were found to be present in Pseudomonas pseudoalcaligenes ATCC 17440. A mutant strain with 31-fold reduced orotate phosphoribosyltransferase (encoded by pyrE) activity was isolated that exhibited a pyrimidine requirement for uracil or cytosine. Uptake of the nucleosides uridine or cytidine by wild-type or mutant cells was not detectable; explaining the inability of the mutant strain to utilize either nucleoside to satisfy its pyrimidine requirement. When the wildtype strain was grown in the presence of uracil, the activities of the five de novo enzymes were depressed. Pyrimidine limitation of the mutant strain led to the increase in aspartate transcarbamoylase and dihydroorotate dehydrogenase activities by more than 3-fold, and dihydroorotase and orotidine 5′-monophosphate decarboxylase activities about 1.5-fold, as compared to growth with excess uracil. It appeared that the syntheses of the de novo enzymes were regulated by pyrimidines. In vitro regulation of aspartate transcarbamoylase activity in P. pseudoalcaligenes ATCC 17440 was investigated using saturating substrate concentrations; transcarbamoylase activity was inhibited by Pi, PPi, uridine ribonucleotides, ADP, ATP, GDP, GTP, CDP, and CTP.
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  • 2
    ISSN: 1432-0800
    Source: Springer Online Journal Archives 1860-2000
    Topics: Energy, Environment Protection, Nuclear Power Engineering , Medicine
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-0800
    Source: Springer Online Journal Archives 1860-2000
    Topics: Energy, Environment Protection, Nuclear Power Engineering , Medicine
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Sedimentology 41 (1994), S. 0 
    ISSN: 1365-3091
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Geosciences
    Notes: The only reported occurrence of quartz-rich sands in Jamaica is on the plains of Black River, St Elizabeth, where they outcrop in isolated pockets. The sands overlie limestones of the White Limestone Supergroup and the Coastal Group, and partly underlie Holocene peat deposits.Monocrystalline quartz, containing fluid and mineral inclusions, is the dominant mineral of the sands, with the heavy minerals. magnetite, haematite, epidote, rutile, anatase, zircon and tourmaline, occurring in minor amounts. Grain surface texture studies of the quartz grains have identified a series of mechanical and chemical features. Microtextures depicting marine, aeolian and pedological environments have been retained on the grains and represent the last three stages in the history of the grains.The petrography of the sands indicates an igneous provenance, with the major source of the detrital minerals being the Cretaceous granitoids that outcrop in the eastern half of the island. These rocks were unroofed during the uplift of Jamaica in the Late Tertiary and were subjected to extensive chemical weathering, which accounted for the breakdown of the majority of their primary silicate minerals. Fluvial transportation and deposition of detritus onto the shelf of the south coast commenced during this period and continued into the Pleistocene, providing terrigenous sand that was modified along the coast to quartz arenite by moderate to high energy marine conditions. Tidal currents, east-west longshore currents and weathering contributed to the maturity of the sand by the time it had been transported along the shelf to the vicinity of Black River. During low sea level stands in the Pleistocene, some of this sediment that became trapped on the shelf was blown inland by south-east winds.
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  • 5
    ISSN: 1432-072X
    Keywords: Thymidylate synthetase ; Trimethoprim ; Thymidine auxotrophy ; Xanthomonas maltophilia ; Thymidine phosphorylase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Thymidylate synthetase mutants of Xanthomonas maltophilia ATCC 13270 were isolated on a solid minimal medium containing 50 mg/l thymidine and a high concentration of trimethoprim (500 mg/l). It was found that a high concentration of trimethoprim was required to prevent background growth of the wild-type strain. The isolated mutants could grow on thymidine or dTMP at a concentration of 50 mg/l while they were unable to grow on 1000 mg/l thymine or 50 mg/l deoxyridine. Thymidylate synthetase activity was assayed in the wild-type cells and in the mutant cells but only the wild-type cells contained measurable enzyme activity.
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 154 (1990), S. 407-409 
    ISSN: 1432-072X
    Keywords: Pyrimidine biosynthesis ; Pseudomonas cepacia ; Transposon mutagenesis ; Aspartate transcarbamoylase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Pyrimidine biosynthesis was investigated in Pseudomonas cepacia ATCC 17759. The presence of the de novo pyrimidine biosynthetic pathway enzyme activities was confirmed in this strain. Following transposon mutagenesis of the wild-type cells, a mutant strain deficient for orotidine 5′-monophosphate decarboxylase activity (pyrF) was isolated. Uracil, cytosine or uridine supported the growth of this mutant. Uracil addition to minimal medium cultures of the wild-type strain diminished the levels of the de novo pyrimidine biosynthetic enzyme activities, while pyrimidine limitation of the mutant cells increased those de novo enzyme activities measured. It was concluded that regulation of pyrimidine biosynthesis at the lelel of enzyme synthesis in P. cepacia was present. Aspartate transcarbamoylase activity was found to be regulated in the wild-type cells. Its activity was shown to be controlled in vitro by inorganic pyrophosphate, adenosine 5′-triphosphate and uridine 5′-phosphate.
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  • 7
    ISSN: 1432-072X
    Keywords: Dihydropyrimidine dehydrogenase ; Dihydropyrimidinase ; Pyrimidine catabolism ; Pseudomonas chlororaphis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A dihydropyrimidine dehydrogenase mutant of Pseudomonas chlororaphis ATCC 17414 was isolated and characterized in this study. Initially, reductive catabolism of uracil was confirmed to be active in ATCC 17414 cells. Following chemical mutagenesis and d-cycloserine counterselection, a mutant strain unable to utilize uracil as a nitrogen source was identified. It was also unable to utilize thymine as a nitrogen source but could use either dihydrouracil or dihydrothymine as a sole source of nitrogen. Subsequently, it was determined that the mutant strain was deficient for the initial enzyme in the reductive pathway dihydropyrimidine dehydrogenase. The lack of dehydrogenase activity did not seem to have an adverse effect upon the activity of the second reductive pathway enzyme dihydropyrimidinase activity. It was shown that both dihydropyrimidine dehydrogenase and dihydropyrimidinase levels were affected by the nitrogen source present in the growth medium. Dihydropyrimidine dehydrogenase and dihydropyrimidinase activities were elevated after growth on uracil, thymine, dihydrouracil or dihydrothymine as a source of nitrogen.
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 1432-072X
    Keywords: Dihydropyrimidinase ; Purification ; Dihydropyrimidine ; Hydantoin ; Pseudomonas stutzeri
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Dihydropyrimidinase from Pseudomonas stutzeri ATCC 17588 was purified 100-fold and characterized. It was found that dihydrouracil, dihydrothymine and hydantoin could serve as substrates for the partially purified enzyme. The K m values for dihydrouracil, dihydrothymine and hydantoin were determined to be 19.6 μM, 21.3 μM and 36.4 μM, respectively, while their respective V max values were 0.836 μmol/min, 0.666 μmol/min and 2.21 μmol/min. Between pH 7.5 and 9.0, enzyme activity was shown to be maximal. The optimum temperature for enzyme activity was 45 °C. Using gel filtration, the molecular weight of the enzyme was calculated to be approximately 115000 Da. Metal ions were found to influence the level of enzyme activity. Dihydropyrimidinase activity was stimulated by magnesium ions and inhibited by either zinc or copper ions.
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  • 9
    Electronic Resource
    Electronic Resource
    Cambridge : Cambridge University Press
    Journal of American studies 17 (1983), S. 131-132 
    ISSN: 0021-8758
    Source: Cambridge Journals Digital Archives
    Topics: English, American Studies , History , Political Science , Sociology , Economics
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 1520-6882
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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