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  • Carbon monoxide  (2)
  • Hyp  (2)
  • Nitrate reductase
  • twins
  • Springer  (5)
  • American Institute of Physics
  • Nature Publishing Group
  • Springer Nature
  • 1980-1984  (5)
Collection
Keywords
Publisher
  • Springer  (5)
  • American Institute of Physics
  • Nature Publishing Group
  • Springer Nature
Years
Year
  • 1
    Electronic Resource
    Electronic Resource
    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
    Keywords: Vitamin D ; Hyp ; X-linked hypophosphatemia ; Metabolic bone disease ; Mice
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02405387
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  • 2
    Electronic Resource
    Electronic Resource
    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
    Keywords: X-linked hypophosphatemia ; Hyp ; Milk ; Phosphate ; Rickets
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02405118
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  • 3
    Electronic Resource
    Electronic Resource
    Thermophilic Bacilli growing with carbon monoxide (1984)
    Springer
    Archives of microbiology 139 (1984), S. 402-408 
    Details
    ISSN: 1432-072X
    Keywords: Carboxydotrophic bacteria ; Bacillus schlegelii ; Species description ; Autotrophic growth ; Thermophilic bacteria ; Carbon monoxide ; Carbon monoxide oxidase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00408387
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  • 4
    Electronic Resource
    Electronic Resource
    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
    Keywords: Nitrobacter hamburgensis ; Nitrite oxidoreductase ; Nitrate reductase ; Molybdenum iron-sulfur protein ; Ultrastructure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00454918
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  • 5
    Electronic Resource
    Electronic Resource
    The cytochrome composition of carboxydotrophic bacteria (1983)
    Springer
    Archives of microbiology 135 (1983), S. 293-298 
    Details
    ISSN: 1432-072X
    Keywords: Carbon monoxide ; Carboxydotrophic bacteria ; Cytochromes ; Electron transport ; CO insensitivity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00413484
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