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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 5 (1960), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Anaesthesia 36 (1981), S. 0 
    ISSN: 1365-2044
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: A system for autologous transfusion of postoperative, mediastinal drainage blood, after cardiopulmonary bypass is described. The method is evaluated for quality of blood, ease of usage and cost.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Science, Ltd
    Anaesthesia 57 (2002), S. 0 
    ISSN: 1365-2044
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Summary Pressures in the cuffs of three commonly used tracheal tubes (Portex Profile Softseal®, Mallinckrodt Lo-Contour® and Mallinckrodt Hi-Contour®, size 8.0 mm and 9.0 mm internal diameter), inflated with air, were measured during simulated ascents in an altitude chamber to 10 000 ft. There was no detectable difference in performance between sizes for each type of tracheal tube. When averaged over the two sizes for each type of tube, cuff pressure reached the␣critical perfusion pressure 50 cmH2O (37 mmHg) for tracheal mucosa at a higher altitude in the Portex Profile Softseal (2837 ft, 95% CI 2488–3186 ft) than in the Mallinckrodt Lo-Contour (2128 ft, 95% CI 1779–2476 ft; p = 0.02) and Mallinckrodt Hi-Contour (1820 ft; 95% CI 1471–2168 ft; p = 0.002) tracheal tubes. When the cuffs of the 9.0-mm tracheal tubes were inflated with saline, much smaller increases in pressure were measured with increasing altitude, although inflation of the cuffs with saline was technically difficult. Commonly used tracheal tubes with air-inflated cuffs can be used for aeromedical retrieval, but air should be evacuated from the cuffs after increases in altitude of as little as 2000–3000 ft.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 338 (1989), S. 628-628 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] SIR-I suggest that there is an alternative explanation for Pimm and Redfearn's1 observations that is consistent with a white-noise hypothesis of environmental variation in terrestrial environments5 - at least over the timescales they examined (up to 30 years). The phenomenon, the standard ...
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Molecular genetics and genomics 255 (1997), S. 302-310 
    ISSN: 1617-4623
    Keywords: Key wordsArabidopsis ; Ubiquitin ; Ubiquitin-specific protease
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The ubiquitin-specific proteases (UBPs) are a class of enzymes vital to the ubiquitin pathway. These enzymes cleave ubiquitin at its C-terminus from two types of substrates containing (i) ubiquitin in an α-amino linkage, as found in the primary ubiquitin translation products, polyubiquitin and ubiquitin-ribosomal fusion proteins, or (ii) ubiquitin in an ɛ-amino linkage, as found in multiubiquitin chains either unattached or conjugated to cellular proteins. We have isolated cDNAs for two Arabidopsis thaliana genes, AtUBP3 and AtUBP4, which encode UBPs that are 93% identical. These two cDNAs represent the only two members of this subgroup and encode the smallest UBPs described to date in any organism. Using in vivo assays in Escherichia coli that allow the coexpression of a UBP with a putative substrate, we have shown that AtUBP3 and AtUBP4 can specifically deubiquitinate the artificial substrate Ub-X-β-gal but cannot act upon the natural α-amino-linked ubiquitin fusions Arabidopsis Ub-CEP52 and Arabidopsis polyubiquitin. Affinity-purified antibody prepared against AtUBP3 expressed in E. coli recognizes both AtUBP3 and AtUBP4. AtUBP3 and/or AtUBP4 are present in all Arabidopsis organs examined and at multiple developmental stages. Subcellular localization studies show that AtUBP3 and/or AtUBP4 are present in nuclear extracts. Possible physiological roles for these UBPs are discussed.
    Type of Medium: Electronic Resource
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