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  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Nuclear Physics, Section B 381 (1992), S. 544-558 
    ISSN: 0550-3213
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Physics
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1365-2133
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The effect of systemic glucocorticoid treatment on collagen synthesis in patients with various dermatoses was studied by measuring the carboxyterminal propeptide of type I procollagen (PICP) and the aminoterminal propeptide of type III procollagen (PIIINP) in serum. Changes in the propeptide concentrations were compared with those of osteocalcin, which reflects osteoblastic activity, and tartrate resistant acid phosphatase (TRAP), which reflects osteoclastic activity. The treatment caused significant decreases in levels of PICP, PIIINP and osteocalcin of 38, 34 and 49%, respectively (P〈0.001). For TRAP, both increases and decreases were seen. The effects on PICP and PIIINP were evident 2–4 days after the onset of steroid therapy. The decreases in PICP was dose-related (r=0.470, P〈0.005) but even relatively small doses (0.1 mg of prednisone/kg/1 day) caused a significant reduction in PICP. After cessation of treatment, the levels of PICP returned to the pretreatment level in 1 week. The present study demonstrates that systemic glucocorticoid therapy in humans suppresses the synthesis of type I and III collagens and also non-collagenous bone matrix proteins.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Journal of Psychosomatic Research 37 (1993), S. 643-652 
    ISSN: 0022-3999
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Medicine , Psychology
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Physics Letters B 297 (1992), S. 327-330 
    ISSN: 0370-2693
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Physics
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Histochemistry and cell biology 83 (1985), S. 231-235 
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Three different isoenzymes of human carbonic anhydrase are now well characterized. Carbonic anhydrase I and II have been known for several years and are located in high amounts in red blood cells as well as in many other tissues. Carbonic anhydrase III, a protein showing CO2 hydratase and p-nitrophenylphosphatase activity was isolated from skeletal muscle some years ago. Earlier observations based on enzyme activity and radioimmunoassay studies have suggested that this protein is present in greater quantities in red skeletal muscles than in white ones. We have purified CA III from human soleus muscle and using obtained monospecific polyclonal antibody localized this protein in the same muscle fibers which show acid resistant ATPase activity. Using this protein as a marker for type I muscle fibers, fiber classification into type I and II could now be done also from paraffin embedded sections.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1432-2013
    Keywords: Oxygen uptake ; Blood lactate ; Blood acid base balance ; Endurance running ; Serum myoglobin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The effects of 30 min running with stepwise increasing intensity (exhaustive, energy demand approx. 50 → 100% ofVO2max), 60 s supramaximal running (anaerobic, ≥125% ofVO2max) and 40–60 min low-intensity running (acrobic, 40–60% ofVO2max) on serum concentration of muscle-derived proteins were studied in 5 male and 5 female elite orienteerers. S-Carbonic anhydrase III (S-CA III) was used as a marker of protein leakage from type I (slow oxidative) muscle fibres and S-myoglobin (S-Mb) as a non-selective (type I+II) muscular marker. The fractional increase in S-CA III (ΔS-Ca III) was 0.37±0.09 (mean±SEM,p〈0.001), 0.10±0.05 (N. S.) and 0.46±0.09 (p〈0.001) 1 h after exhaustive, anaerobic and aerobic exercise, respectively. The corresponding values for ΔS-Mb were 1.45±0.36 (p〈0.001), 0.39±0.13 (p〈0.01) and 0.67±0.18 (p〈0.001). The value for the ΔS-CA III/ΔS-Mb ratio was 0.68±0.03 after the acrobic exercise, but only 0.25–0.26 (p vs. aerobic exercise 〈0.001) after the two high-intensity forms of exercise. Since type I fibres of skeletal muscle are known to be responsible for power production during low-intensity exercise, whereas fibres of both type I and type II are active at higher intensities, the ΔS-CA III/ΔS-Mb ratio may depend on the recruitment profile of type I vs. type I+II fibres.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Carbonic anhydrase (CA III) and myoglobin contents from isolated human muscle fibers were quantified using a sensitive time-resolved fluoroimmunoassay. Human psoas muscle specimens were freeze-dried, and single fibers were dissected out and classified into type I, IIA and IIB by myosin ATPase staining. Fiber typing was further confirmed by SDS-PAGE. CA III and myoglobin were found in all fiber types. Type I fibers contained higher concentrations of CA III and myoglobin than type IIA and IIB fibers. The relative concentrations of CA III in type IIA and IIB fibers were respectively 24% and 10% of that in type I fibers. The relative concentrations of myoglobin in type IIA and IIB fibers were 60% and 28% of that in type I fibers. Anti-CA III immunoblotting results from fiber-specific pooled samples agreed well with quantitative measurements. The results indicate that CA III is a more specific marker than myoglobin for type I fibers.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Advances in contraception 5 (1989), S. 47-49 
    ISSN: 1573-7195
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Resumé Ce rapport concerne un cas unique de perforation de l'utérus et de la vessie par un dispositif intra-utérin au cuivre (Nova-T). La patiente souffrant de cystite récidivante, une cystoscopie a été pratiquée, ce qui a permis de constater que le bras horizontal du DIU avait pénétré dans la vessie. Le DIU a été enlevé par le vagin en tirant sur les fils de localisation. La patiente s'est rétablie sans complications. Ce cas montre que les DIU de seconde génération peuvent occasionner une perforation de la vessie.
    Abstract: Resumen Presentamos un caso único de perforación uterina y de vejiga por un dispositivo intrauterino de cobre (Nova-T). La paciente se presentó con cistitis recurrente lo que condujo a una cistoscopía donde el brazo del DIU fue visto en la vejiga. E1 DIU fue quitado vaginalmente tirando de los hilos localizadores. La paciente se recuperó sin complicaciones. El caso demuestra que también las nuevas, segundas generaciones de DIU pueden causar perforación de vejiga.
    Notes: Abstract We report a unique case of uterine and bladder perforation by a copper intrauterine device (Nova-T). The patient presented with recurrent cystitis, which led to cystoscopy, where the horizontal arm of the IUD was seen intravesically. The IUD was removed vaginally by pulling the locator strings. The patient recovered without complications. The case shows that the new, second-generation IUDs may also cause bladder perforation.
    Type of Medium: Electronic Resource
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