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  • Nitrate reductase  (7)
  • Carbon monoxide  (6)
  • twins  (5)
  • Hyp
  • Springer  (20)
  • American Institute of Physics
  • Nature Publishing Group
  • Springer Nature
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Schlagwörter
Verlag/Herausgeber
  • Springer  (20)
  • American Institute of Physics
  • Nature Publishing Group
  • Springer Nature
  • Wiley-Blackwell  (1)
Erscheinungszeitraum
  • 1
    Digitale Medien
    Digitale Medien
    Metabolites of vitamin D in normal and X-linked hypophosphatemic mice (1984)
    Springer
    Calcified tissue international 36 (1984), S. 662-667 
    Details
    ISSN: 1432-0827
    Schlagwort(e): Vitamin D ; Hyp ; X-linked hypophosphatemia ; Metabolic bone disease ; Mice
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Medizin , Physik
    Notizen: Summary Hyp mice are a model for human X-linked hypophosphatemia (vitamin D-resistant rickets.) To determine whether an abnormality of vitamin D metabolism exists in this disease, the profiles of the metabolites of vitamin D were determined in normal andHyp mouse plasma.Hyp and normal mice were fed a vitamin D-deficient diet and received 1,23H-vitamin D3 at 16 Ci/mmol by stomach tube at 5 ng/g body weight (0.21 µCi/g b.w.) on alternate days for 14 days. The dose of vitamin D given maintained near normal plasma 25-OH-vitamin D. Thus the mice were in a vitamin D-replete state with all metabolite pools labeled with3H. Plasma was collected from 4 normal and 4Hyp mice. The plasma was extracted, and the extracts were chromatographed separately for each mouse on an LH-20 column. Each major peak of radioactivity was rechromatographed using high performance liquid chromatography on a Zorbax-Sil column using solvent systems known to resolve several vitamin D metabolites. Twenty-one radioactive peaks were identified. The disintegrations per minute of3H in each peak were quantified and converted to plasma concentration using the known specific activity of the administered vitamin D. The 25-OH-vitamin D accounted for 55% of the circulating radioactivity, and 24,25-(OH)2-vitamin D accounted for 22%. The plasma levels of 24,25-(OH)2-vitamin D were similar to levels previously reported by us using protein binding assays. No peaks of radioactivity were missing in the plasma extracts of theHyp mice. Also there was no evidence that plasma 24,25-(OH)2-vitamin D was elevated in theHyp mice.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF02405387
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  • 2
    Digitale Medien
    Digitale Medien
    Normal milk composition in lactating X-linked hypophosphatemic mice despite continued hypophosphatemia (1983)
    Springer
    Calcified tissue international 35 (1983), S. 750-754 
    Details
    ISSN: 1432-0827
    Schlagwort(e): X-linked hypophosphatemia ; Hyp ; Milk ; Phosphate ; Rickets
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Medizin , Physik
    Notizen: Summary Patients with X-linked hypophosphatemia and mice bearing theHyp gene have reduced renal tubular reabsorption of phosphate and an osteomalacic bone disease. To test if altered phosphate transport also exists in the mammary glands, milk was analyzed from normal (n=9) and heterozygousHyp (n=8) mice 14 days after giving birth. Inorganic phosphate, total phosphate, calcium, magnesium, sodium, and potassium were measured; percent cream, fat, water, and nonfat organic solids were measured; and protein was measured. No significant differences (NSD) were found except for greater sodium inHyp milk. There was also NSD in litter weight. The lactatingHyp had a lower body weight and remained hypophosphatemic relative to lactating normals, but both groups had higher plasma phosphate than nonlactating controls of the same genotype. The data suggest thatHyp mice can accumulate a normal amount of phosphate in their milk despite the plasma phosphate being two-thirds of normal. These data, with other recent reports of different organ systems, suggest that the altered phosphate transport activity may be restricted to the kidney.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF02405118
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  • 3
    Digitale Medien
    Digitale Medien
    Thermophilic Bacilli growing with carbon monoxide (1984)
    Springer
    Archives of microbiology 139 (1984), S. 402-408 
    Details
    ISSN: 1432-072X
    Schlagwort(e): Carboxydotrophic bacteria ; Bacillus schlegelii ; Species description ; Autotrophic growth ; Thermophilic bacteria ; Carbon monoxide ; Carbon monoxide oxidase
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract Four strains of obligately thermophilic Bacilli capable of growing with carbon monoxide as a sole carbon and energy source were isolated from settling ponds of a sugar factory. Most of them could be identified as strains of Bacillus schlegelii on the basis of cell wall composition, DNA homology menaquinone and DNA base content. Growth with CO was very fast (t d =3 h) and was optimal at 65°C. No growth occurred below 50°C. As with the mesophilic carboxydotrophs, hydrogen plus carbon dioxide could also serve as autotrophic substrates. Growth of the isolates with CO depended on the presence of molybdenum in the growth medium. This suggested CO oxidase in the newly isolated Bacilli being a molybdenum hydroxylase similar to the enzymes from the mesophilic carboxydotrophs. Some data characterizing the CO-oxidizing activity in extracts of the thermophilic isolates are also provided.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00408387
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  • 4
    Digitale Medien
    Digitale Medien
    The periplasmic nitrate reductase of Rhodobacter capsulatus; purification, characterisation and distinction from a single reductase for trimethylamine-N-oxide, dimethylsulphoxide and chlorate (1987)
    Springer
    Archives of microbiology 147 (1987), S. 340-345 
    Details
    ISSN: 1432-072X
    Schlagwort(e): Rhodobacter capsulatus ; Periplasmic enzymes ; Nitrate reductase ; Trimethylamine-N-oxide/dimethylsulphoxide/chlorate reductase ; Molybdenum cofactor
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract The periplasmic dissimilatory nitrate reductase from Rhodobacter capsulatus N22DNAR+ has been purified. It comprises a single type of polypeptide chain with subunit molecular weight 90,000 and does not contain heme. Chlorate is not an alternative substrate. A molybdenum cofactor, of the pterin type found in both nitrate reductases and molybdoenzymes from various sources, is present in nitrate reductase from R. capsulatus at an approximate stoichiometry of 1 molecule per polypeptide chain. This is the first report of the occurrence of the cofactor in a periplasmic enzyme. Trimethylamine-N-oxide reductase activity was fractionated by ion exchange chromatography of periplasmic proteins. The fractionated material was active towards dimethylsulphoxide, chlorate and methionine sulphoxide, but not nitrate. A catalytic polypeptide of molecular weight 46,000 was identified by staining for trimethylamine-N-oxide reductase activity after polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate. The same polypeptide also stained for dimethylsulphoxide reductase activity which indicates that trimethylamine-N-oxide and dimethylsulphoxide share a common reductase.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00406130
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  • 5
    Digitale Medien
    Digitale Medien
    Reisolation of the carbon monoxide utilizing hydrogen bacterium Pseudomonas carboxydovorans (Kistner) comb. nov. (1978)
    Springer
    Archives of microbiology 118 (1978), S. 35-43 
    Details
    ISSN: 1432-072X
    Schlagwort(e): Autotrophic growth ; Hydrogen ; Carbon monoxide ; Gram-negative hydrogen bacteria ; Pseudomonas carboxydovorans ; Facultative autotrophs ; CO oxidation
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract From enrichment cultures four carbon monoxide utilizing bacteria were isolated; strain OM5 isolated from waste water was studied in detail. The cells are Gram-negative, slightly curved rods, motile by a single subpolarly inserted flagellum. The colonies are smooth, translucent and not slimy. The cells are able to grow autotrophically in mineral medium under an atmosphere of 40% CO, 5% O2 and 55% N2 at a doubling time of 20h (30°C) or of 85% H2, 5% O2 and 10% CO2 at a doubling time of 7h. Heterotrophic growth occurrd on organic acids such as acetate (t d =8h), pyruvate (t d =8h), lactate, crotonate, malate, succinate (t d =8h), formate (t d =35h) and glyoxylate as substrates. The enzyme system for carbon monoxide utilization is formed only during growth on CO; hydrogenase is present in cells grown on CO or on H2+CO2 as well as grown on pyruvate. The rate of oxygen reduction by intact CO-grown cells is 3.7-fold higher in the presence of hydrogen than in the presence of carbon monoxide. During growth the stoichiometry of gas uptake was 6.1 CO+2.8 O2+H2O → 〈CH2O〉+5.1 CO2. For the new isolate the name Pseudomonas carboxydovorans (Kistner) comb. nov. has been proposed.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00406071
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  • 6
    Digitale Medien
    Digitale Medien
    Membrane-bound nitrite oxidoreductase of Nitrobacter: evidence for a nitrate reductase system (1984)
    Springer
    Archives of microbiology 140 (1984), S. 153-158 
    Details
    ISSN: 1432-072X
    Schlagwort(e): Nitrobacter hamburgensis ; Nitrite oxidoreductase ; Nitrate reductase ; Molybdenum iron-sulfur protein ; Ultrastructure
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract Nitrite oxidoreductase, the essential enzyme complex of nitrite oxidizing membranes, was isolated from cells of the nitrifying bacterium Nitrobacter hamburgensis. The enzyme system was solubilized and purified in the presence of 0.25% sodium deoxycholate. Nitrite oxidoreductase oxidized nitrite to nitrate in the presence of ferricyanide. The pH optimum was 8.0, and the apparent K m value for nitrite amounted to 3.6 mM. With reduced methyl-and benzylviologen nitrite oxidoreductase exhibited nitrate reductase activity with an apparent K m value of 0.9 mM for nitrate. NADH was also a suitable electron donor for nitrate reduction. The pH optimum was 7.0. Treatment with SDS resulted in the dissociation into 3 subunits of 116,000, 65,000 and 32,000. The enzyme complex contained iron, molydbenum, sulfur and copper. A c-type cytochrome was present. Isolated nitrite oxidoreductase is a particle of 95±30 Å in diameter.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00454918
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  • 7
    Digitale Medien
    Digitale Medien
    CO2 is the first species formed upon CO oxidation by CO dehydrogenase from Pseudomonas carboxydovorans (1986)
    Springer
    Archives of microbiology 145 (1986), S. 358-360 
    Details
    ISSN: 1432-072X
    Schlagwort(e): Carbon monoxide ; Carbon dioxide ; CO dehydrogenase ; Carbonic anhydrase ; Pseudomonas carboxydovorans
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract The active species of “CO2”, i.e. CO2 or HCO 3 - , formed in the CO dehydrogenase reaction was determined using the pure enzyme from the carboxydotrophic bacterium Pseudomonas carboxydovorans. Employing an assay system similar to that used to test for carbonic anhydrase, data were obtained which are quite compatible with those expected if CO2 is the first species formed. In addition, carbonic anhydrase activity was not detected in P. carboxydovorans.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00470871
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  • 8
    Digitale Medien
    Digitale Medien
    The cytochrome composition of carboxydotrophic bacteria (1983)
    Springer
    Archives of microbiology 135 (1983), S. 293-298 
    Details
    ISSN: 1432-072X
    Schlagwort(e): Carbon monoxide ; Carboxydotrophic bacteria ; Cytochromes ; Electron transport ; CO insensitivity
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract Spectroscopy at room and liquid nitrogen temperatures with extracts of the carbon monoxide-oxidizing bacteria Pseudomonas carboxydovorans, P. carboxydohydrogena, P. carboxydoflava, P. compransoris, Alcaligenes carboxydus, and Arthrobacter 11/x revealed the presence of normal electron transport systems, containing b-, c-, and a-type cytochromes at concentrations that compare to those of other aerobic bacteria. CO did not induce the formation of special CO-insensitive terminal oxidases. The gross composition of the respiratory chains was not affected by the type of growth substrate, and cytochrome d(=a2) was not detected. However, certain b-type cytochromes were only found when CO or H2 + CO2 served as growth substrates. All strains contained at least two different b-type cytochromes. Cytochrome b563 formed a weak CO-complex and was identified as a novel cytochrome o. It functions as CO-insensitive, alternative terminal oxidase in carboxydotrophic bacteria. A soluble CO-binding cytochrome c was present in P. carboxydovorans, P. carboxydohydrogena, and P. carboxydoflava. A CO-binding protoheme compound could be identified as catalase in P. compransoris, P. carboxydovorans, P. carboxydohydrogena, A. carboxydus, and Arthrobacter 11/x. The data are consistent with the presence of branched respiratory chains in the carboxydotrophs examined, and suggest the functioning of both, cytochrome a and the novel cytochrome o as terminal oxidases.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00413484
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  • 9
    Digitale Medien
    Digitale Medien
    Plasmids in carboxydotrophic bacteria: physical and restriction analysis (1988)
    Springer
    Archives of microbiology 149 (1988), S. 540-546 
    Details
    ISSN: 1432-072X
    Schlagwort(e): Carbon monoxide ; Autotrophic bacteria ; Carboxydotrophic bacteria ; Plasmids ; Restriction analysis ; Mutants ; Deletion
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract Twenty species and strains of aerobic CO-oxidizing bacteria were screened for the occurrence of plasmids. Six of them harbored plasmids between 45 and 558kb. Megaplasmids of 428 and 558 kb were resolved in Alcaligenes carboxydus. Restriction digest patterns of plasmids from different carboxydotrophic bacteria were dissimilar. However, the patterns obtained with the plasmids from the strains OM5, OM4 and OM2 of Pseudomonas carboxydovorans were very much the same. The nine cured mutants of P. carboxydovorans OM5, as well as the deletion mutant OM5-29, could not grow chemolithotrophically with CO or H2 plus CO2, as they were devoid of CO dehydrogenase, hydrogenase and ribulose bisphosphate carboxylase. The deletion mutant OM5-24 retained the ability to grow with CO. It could not grow with H2 plus CO2 and was devoid of H2ase. The data suggest the residence of structural and/or regulatory genes of CODH, H2ase and RuBPCx on plasmid pHCG3 of P. carboxydovorans.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00446758
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  • 10
    Digitale Medien
    Digitale Medien
    The structural genes encoding CO dehydrogenase subunits (cox L, M and S) in Pseudomonas carboxydovorans OM5 reside on plasmid pHCG3 and are, with the exception of Streptomyces thermoautotrophicus, conserved in carboxydotrophic bacteria (1992)
    Springer
    Archives of microbiology 157 (1992), S. 301-304 
    Details
    ISSN: 1432-072X
    Schlagwort(e): Carbon monoxide ; CO ; Carboxydotrophic bacteria ; Plasmids ; CO Dehydrogenase ; Deoxyoligonucleotides ; Cox ; Pseudomonas carboxydovorans ; Pseudomonas carboxydohydrogena ; Pseudomonas carboxydoflava ; Streptomyces thermoautotrophicus ; Pseudomonas thermocarboxydovorans ; Bacillus schlegelii ; Alcaligenes carboxydus ; Arthrobacter ; Azomonas
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract Employing deoxyoligonucleotide probes and Southern hybridizations, we have examined in carboxydotrophic bacteria the localization on the genome of genes encoding the large, medium and small subunits of CO dehydrogenase (coxL, M and S, respectively). In Pseudomonas carboxydovorans OM5 coxL, M and S were identified on the plasmid pHCG3; they were absent on the chromosome. This was evident from positive hybridizations with plasmid DNA of the wild-type strain OM5 and the absence of hybridizations with chromosomal DNA from the plasmid cured mutant strain OM5–12. The genes coxL, M and S were found on plasmids in all other plasmid-containing carboxydotrophic bacteria e.g. Alcaligenes carboxydus, Azomonas B1, Pseudomonas carboxydoflava, Pseudomonas carboxydovorans OM2 and OM4. Cox L, M and S could be identified on the chromosome of the plasmid-free bacteria Arthrobacter 11/x, Bacillus schlegelii, Pseudomonas carboxydohydrogena, and Pseudomonas carboxydovorans OM3. These results essentially confirm and extend former reports that cox genes are rather conserved among carboxydotrophic bacteria of distinct taxonomic position. However, Streptomyces thermoautotrophicus is an noteworthy exception since none of the three cox genes could be detected. This refers to a new type of CO dehydrogenase and is in accord with results indicating that the S. thermoautotrophicus CO dehydrogenase has an unusual electron acceptor specificity and some other properties setting it apart from the ‘classical’ CO dehydrogenases.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00245166
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