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  • Blackwell Publishing Ltd  (9)
  • 1995-1999  (8)
  • 1965-1969  (1)
  • 1
    Digitale Medien
    Digitale Medien
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 150 (1968), S. 0 
    ISSN: 1749-6632
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Allgemeine Naturwissenschaft
    Notizen: (1) Of the 27 burn fatalities with respiratory tract involvement, this internal damage was the primary cause of death in 20 cases.(2) The edema and sodium contents in the lungs become maximal in 12 to 48 hr following the burn.(3) The surface tension in the lungs is abnormally elevated in respiratory burns and may be one of the causes of nonobstructive atelectasis.(4) The venous clotting time becomes depressed in the acute phase of respiratory burn and returns to normal in 24 hr.(5) Lymph drainage into the left thoracic duct vestibule decreases during the acute phase of the burn in the dog.(6) In the acute phase of the burn, the respiratory insufficiency is secondary to edema and to patchy atelectasis which can be reduced by automatic positive pressure respiration.(7) Infection of pulmonary and tracheobronchial tree plays a major role after 48 hr and early antibiotic coverage may help to control it.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Oxford, UK : Blackwell Publishing Ltd
    Plant, cell & environment 22 (1999), S. 0 
    ISSN: 1365-3040
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Biologie
    Notizen: 
 IWF, intercellular washing fluid
 pCMB, p-chloromercuribenzoic acid
 SNAP, S-nitroso-N-acetyl-penicillamine SNP, sodium nitroprusside
 TMB, 3,3’,5,5’- tetramethylbenzidine

 Sodium nitroprusside (SNP) and S-nitroso-N-acetyl-penicillamine (SNAP) are two nitric oxide (NO)-releasing compounds that, when used at 5·0 mol m–3 concentrations, are capable of releasing NO in the aqueous phase at a rate of 35 ± 4 and 47 ± 5 μmol m–3 s–1, respectively. For this reason, the effect of SNP and SNAP on coniferyl alcohol peroxidase and on H2O2 production by the lignifying xylem of Zinnia elegans (L.) has been studied in order to ascertain whether NO, which is a synchronizing chemical messenger in animals and an air pollutant, has any effect on these plant-specific metabolic aspects. The results showed that both SNP and SNAP provoke an inhibition in the mol m–3 concentration range of the coniferyl alcohol peroxidase activity of a basic peroxidase isoenzyme present in the intercellular washing fluid of Z. elegans. The effect of these NO-releasing compounds on peroxidase was confirmed through histochemical studies, which showed that xylem peroxidase was totally inhibited by treatment with these NO donors at 5·0 mol m–3, and by NO at a concentration change rate of 55 ± 5 and 110 ± 9 μmol m–3 s–1. However, SNP, at 5·0 mol m–3, does not have any effect on H2O2 production by the xylem of Z. elegans. The fact that SNP and SNAP are two structurally dissimilar compounds which only share the common ability to release NO in aqueous buffer, and that similar results were obtained when using NO itself, suggest that NO could be considered as an inhibitor of coniferyl alcohol peroxidase which does not affect H2O2 production in the xylem of Z. elegans.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 3
    Digitale Medien
    Digitale Medien
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 159 (1998), S. 0 
    ISSN: 1574-6968
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Biologie
    Notizen: An NAD-specific glutamate dehydrogenase from Thermus thermophilus HB8 was purified 350-fold by a several-step procedure involving Blue-Sepharose chromatography. The native protein had a molecular mass of approximately 289 kDa, and consisted of six subunits with a molecular mass of 48 kDa each. The optimum pH for the deaminating reaction was 8.0. The optimum temperature was around 85–90°C. NAD-glutamate dehydrogenase showed a high coenzyme specificity, catalysed preferentially glutamate catabolism and presented Km values for NAD and l-glutamate of 0.27±0.03 mM and 49±10 mM, respectively. No activity was detected with NADH or NADPH, 2-oxoglutarate and ammonia. Enzyme activity was found to be very stable at 72°C. Differential scanning calorimetry revealed a tm of 95°C for denaturation.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 4
    Digitale Medien
    Digitale Medien
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 782 (1996), S. 0 
    ISSN: 1749-6632
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Allgemeine Naturwissenschaft
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 5
    Digitale Medien
    Digitale Medien
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 143 (1996), S. 0 
    ISSN: 1574-6968
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Biologie
    Notizen: Abstract Gentisate 1,2-dioxygenase (E.C.I.14.13) was purified to homogeneity from Klebsiella pneumoniae M5a1, a soil bacterium able to degrade a great variety of aromatic compounds. The molecular mass of the purified holoenzyme was 159 kDa and its structure was deduced to be a tetramer with 38 kDa per subunit. Gentisate 1,2-dioxygenase appears to contain Fe2+ in its active site. The optimum temperature for enzyme activity was estimated to be 30 °C, the optimum pH values varied between 8 and 9 and the isoelectric point was 4.7. Gentisate dioxygenase exhibited typical saturation kinetics and had an apparent Km of 52 μM for gentisate. Its amino acid content was determined to be very similar to that of the enzyme from Pseudomonas acidovorans.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 6
    Digitale Medien
    Digitale Medien
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 135 (1996), S. 0 
    ISSN: 1574-6968
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Biologie
    Notizen: Abstract The streptococcal transposons Tn916 and Tn925 were transferred to several strains of Leuconostoc (Ln.) oenos using the filter mating method. The insertion of both transposons into the chromosome occurred at different sites. Transconjugants of Ln. oenos carrying Tn916 could serve as donors in mating experiments with Lactococcus lactis LM2301. Further analysis of L. lactis LM2301 transconjugants showed that the insertion of the transposon Tn916 into the chromosome was site-specific. These studies establish a basis for the initiation of genetic studies in this Leuconostoc species since there are no efficient conjugal or transformation systems previously described for this microorganism.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 7
    Digitale Medien
    Digitale Medien
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 126 (1995), S. 0 
    ISSN: 1574-6968
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Biologie
    Notizen: Abstract We isolated 3-hydroxybenzoate-6-hydroxylase (E.C. 1.14.13.), an inducible enzyme that catalyzed the para-hydroxylation of 3-hydroxybenzoate (3-HBA) to 2,5-dihydroxybenzoate, from Klebsiella pneumoniae. Although the enzyme was found to be mainly induced by its substrate, a coordinated induction of 3-hydroxybenzoate hydroxylase and gentisate dioxygenase was also observed in the presence of the product of the reaction. The purified enzyme was a monomer with a molecular mass of 42 000. It contained FAD as a prosthetic group, utilized NADH or NADPH with similar efficiencies and its activity was inhibited by Cu2+, Fe2+ and Hg2+. Other properties, such as induction mechanism and kinetic parameters were also studied. Moreover, for the first time the amino acid composition of a 3-hydroxybenzoate-6-hydroxylase was determined.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 8
    ISSN: 1574-6968
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Biologie
    Notizen: Abstract Leishmania (Leishmania) infantum is the causative agent of both the cutaneous and visceral forms of leishmaniasis in southwest Europe; the dog is the main reservoir. In order to identify the L. (L.) infantum zymodemes present in Spain, a total number of 85 Leishmania stocks isolated from dogs (31), HIV-positive patients (46) with visceral or cutaneous leishmaniasis, a patient with visceral leishmaniasis complicating renal transplantation (1) and immunocompetent patients (7) with visceral or cutaneous leishmaniasis, have been characterized by isoenzyme typing. All canine stocks were MON-1, which is the most widespread zymodeme in the Mediterranean area. In immunocompetent patients three zymodemes were found: MON-1 (2), MON-24 (2) and MON-34 (3). Nine different zymodemes were obtained in stocks from HTV co-infected patients, indicating a higher variability of L. (L.) infantum amongst them: MON-1 (in 21 stocks), MON-24 (7), MON-28 (1), MON-29 (3), MON-33 (7), MON-34 (1) and MON-183 (4). Two new zymodemes, MON-198 (1) and MON-199 (1), were described among HIV patients from Spain. The stock from the renal transplanted patient was MON-1. The exclusive presence of certain zymodemes in immunocompromised patients and their absence in typical cases of cutaneous and visceral
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 9
    Digitale Medien
    Digitale Medien
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 141 (1996), S. 0 
    ISSN: 1574-6968
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Biologie
    Notizen: Abstract An NADP(H)-specific glutamate dehydrogenase of Haloferax mediterranei has been purified to apparent homogeneity and characterised. The purified enzyme was stabilized by glycerol in absence of salt. Glutamate dehydrogenase from Hf. mediterranei is a hexameric enzyme with a native molecular mass of 320 kDa composed of monomers each with a molecular mass of 55 kDa. At pH 8.5 the enzyme has Kms of 0.018, 0.34 and 4.2 mM for NADP+, 2-oxoglutarate and ammonium, respectively. Amino acid composition and sequence of the first 16 residues of the N-terminus have been determined.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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