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  • Carbon monoxide  (4)
  • Nitrate reductase  (4)
  • Hyp
  • twins
  • Springer  (11)
  • American Institute of Physics
  • Nature Publishing Group
  • Springer Nature
  • 1985-1989  (6)
  • 1980-1984  (5)
Collection
Keywords
Publisher
  • Springer  (11)
  • 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
    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
    Keywords: Rhodobacter capsulatus ; Periplasmic enzymes ; Nitrate reductase ; Trimethylamine-N-oxide/dimethylsulphoxide/chlorate reductase ; Molybdenum cofactor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00406130
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  • 5
    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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  • 6
    Electronic Resource
    Electronic Resource
    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
    Keywords: Carbon monoxide ; Carbon dioxide ; CO dehydrogenase ; Carbonic anhydrase ; Pseudomonas carboxydovorans
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00470871
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  • 7
    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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  • 8
    Electronic Resource
    Electronic Resource
    Plasmids in carboxydotrophic bacteria: physical and restriction analysis (1988)
    Springer
    Archives of microbiology 149 (1988), S. 540-546 
    Details
    ISSN: 1432-072X
    Keywords: Carbon monoxide ; Autotrophic bacteria ; Carboxydotrophic bacteria ; Plasmids ; Restriction analysis ; Mutants ; Deletion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00446758
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  • 9
    Electronic Resource
    Electronic Resource
    Resolving causes of developmental continuity or “tracking.” I. Longitudinal twin studies during growth (1988)
    Springer
    Behavior genetics 18 (1988), S. 133-151 
    Details
    ISSN: 1573-3297
    Keywords: genes ; environment ; development ; growth ; twins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Psychology
    Notes: Abstract Models of developmental continuity and change in quantitative phenotypes may be tested using longitudinal data from twins. We illustrate a procedure for establishing the power and required sample sizes for detecting developmental transmission against an alternative common-factor hypothesis. We explore the general effects of different heritabilities, different fidelities of environmental and genetic developmental transmission, and varying numbers of occasions of measurement. In addition, a constraint of wide application is postulated for the action of the environment; either environmental effects are transmitted (learned) and occasion specific or they exert a constant influence which is not transmitted (learned). While the situations we examine are necessarily restricted here, our explorations of power show that, providing that we measure on at least four occasions, it is easy to detect developmental transmission with workable sample sizes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01067836
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  • 10
    Electronic Resource
    Electronic Resource
    Cloning of DNA fragments complementary to tobacco nitrate reductase mRNA and encoding epitopes common to the nitrate reductases from higher plants (1987)
    Springer
    Molecular genetics and genomics 209 (1987), S. 552-562 
    Details
    ISSN: 1617-4623
    Keywords: Nitrate reductase ; cDNA expression cloning ; Tobacco ; Sequence ; Cytochrome b5
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Messenger RNAs encoding the nitrate reductase apoenzyme from tobacco can be translated in a cell-free system. Poly(A)+ mRNA fractions from the 23-32 S area of a sucrose gradient were used to build a cDNA library in the expression vector λgt11 with an efficiency of cloning of approximately 104 recombinants/ng mRNA. Recombinant clones were screened with a rabbit polyclonal antibody directed against the corn nitrate reductase, which cross reacts specifically with the nitrate reductases from dicotyledons. Among 240000 recombinant plaques, eight clones were isolated containing inserts of sizes ranging from 1.6 kb to 2.1 kb and sharing sequence homologies. Seven of these clones contained a common internal 1.6 kb EcoRI fragment. The identity of these clones was confirmed as follows. A fusion protein of 170 kDa inducible by IPTG and recognized by the rabbit nitrate reductase antibody was expressed by a lysogen derived from one of the recombinants. The antibodies binding the fused protein were eluted and shown to be inhibitory to the catalytic activity of tobacco nitrate reductase. Two monoclonal antibodies directed against nitrate reductase were also able to bind the hybrid protein. The 1.6 kb EcoRI fragment was sequenced by the method of Sanger. The open reading frame corresponding to a translational fusion with the β-galactosidase coding sequence of the vector shared strong homology at the amino acid level with the heme-binding domain of proteins of the cytochrome b5 superfamily and with human erythrocyte cytochrome b5 reductase. When the 1.6 kb EcoRI fragment was used as a probe for Northern blot experiments a signal corresponding to a 3.5 kb RNA was detected in tobacco and in Nicotiana plumbaginifolia mRNA preparations but no cross-hybridization with corn mRNAs was detected. The probe hybridized with low copy number sequences in genomic blots of tobacco DNA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00331162
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